https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&feed=atom&action=history
Carbohydrate Binding Module Family 44 - Revision history
2024-03-28T21:45:29Z
Revision history for this page on the wiki
MediaWiki 1.35.10
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17011&oldid=prev
Elizabeth Ficko-Blean at 08:25, 11 January 2023
2023-01-11T08:25:19Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:25, 11 January 2023</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>{{<del class="diffchange diffchange-inline">UnderConstruction</del>}}</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>{{<ins class="diffchange diffchange-inline">CuratorApproved</ins>}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: [[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Responsible Curator]]: [[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]</div></td></tr>
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Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17009&oldid=prev
Harry Brumer: changed to standard PDB link template ( Template:PDBlink )
2023-01-10T16:02:43Z
<p>changed to standard PDB link template ( Template:PDBlink )</p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:02, 10 January 2023</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|200px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([<del class="diffchange diffchange-inline">https://www.rcsb.org/structure/</del>2c26 PDB <del class="diffchange diffchange-inline">2C26</del>]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|200px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([<ins class="diffchange diffchange-inline">{{PDBlink}}</ins>2c26 PDB <ins class="diffchange diffchange-inline">2c26</ins>]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase ''Ct''Cel9D-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([<del class="diffchange diffchange-inline">https://www.rcsb.org/structure/</del>2c26 PDB <del class="diffchange diffchange-inline">2C26</del>]) <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([<ins class="diffchange diffchange-inline">{{PDBlink}}</ins>2c26 PDB <ins class="diffchange diffchange-inline">2c26</ins>]) <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17006&oldid=prev
Elizabeth Ficko-Blean at 08:42, 10 January 2023
2023-01-10T08:42:51Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:42, 10 January 2023</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM44, from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum''), targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM44, from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum''), targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a <ins class="diffchange diffchange-inline">[[Carbohydrate-binding_modules#Types|</ins>type B<ins class="diffchange diffchange-inline">]] </ins>CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17005&oldid=prev
Elizabeth Ficko-Blean at 08:41, 10 January 2023
2023-01-10T08:41:51Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:41, 10 January 2023</td>
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<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM44, from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum'' <del class="diffchange diffchange-inline"><cite>#Ahsan1996 #Arai2003</cite></del>), targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM44, from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum''), targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17004&oldid=prev
Elizabeth Ficko-Blean at 08:41, 10 January 2023
2023-01-10T08:41:20Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:41, 10 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l18" >Line 18:</td>
<td colspan="2" class="diff-lineno">Line 18:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM44 from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>) targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM44<ins class="diffchange diffchange-inline">, </ins>from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>)<ins class="diffchange diffchange-inline">, </ins>targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17003&oldid=prev
Elizabeth Ficko-Blean at 08:40, 10 January 2023
2023-01-10T08:40:17Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:40, 10 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l18" >Line 18:</td>
<td colspan="2" class="diff-lineno">Line 18:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM44 <ins class="diffchange diffchange-inline">from the CtCel9D-Cel44A enzyme produced by ''Acetivibrio thermocellus'' (formerly ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>) </ins>targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/ß-1,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and is classified as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17002&oldid=prev
Elizabeth Ficko-Blean at 08:34, 10 January 2023
2023-01-10T08:34:46Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:34, 10 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l18" >Line 18:</td>
<td colspan="2" class="diff-lineno">Line 18:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Ligand specificities ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/<del class="diffchange diffchange-inline">ß1</del>,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and <del class="diffchange diffchange-inline">thus classifies </del>as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>CBM44 targets ß-1,4-polymers such as xyloglucan and cellulose (hydroxyethylcellulose and Avicel), mixed linkage ß-1,3/<ins class="diffchange diffchange-inline">ß-1</ins>,4- glucans (lichenan and barley) or glucomannan (konjac) <cite>Najmudin2006</cite> and <ins class="diffchange diffchange-inline">is classified </ins>as a type B CBM. Affinity for xylan was very low and binding to laminarin, curdlan, pullulan, pustulan, galactomannan or galactan was negative. Isothermal titration calorimetry (ITC) revealed highest affinity for xyloglucan as a polysaccharide (~81.6 x 10<sup>4</sup> M<sup>-1</sup>), which was comparable to the affinity for cellohexaose as an oligosaccharide (~72.8 x 10<sup>4</sup> M<sup>-1</sup>). For other cello-oligosaccharides, this affinity decreased with decreasing chain length, while no binding was detected for cellotriose <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=17001&oldid=prev
Marie-Katherin Zuehlke at 08:21, 10 January 2023
2023-01-10T08:21:25Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:21, 10 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l23" >Line 23:</td>
<td colspan="2" class="diff-lineno">Line 23:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding (Figure 1), as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|<del class="diffchange diffchange-inline">300px</del>|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|<ins class="diffchange diffchange-inline">200px</ins>|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td></tr>
</table>
Marie-Katherin Zuehlke
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=16998&oldid=prev
Marie-Katherin Zuehlke at 16:22, 9 January 2023
2023-01-09T16:22:16Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:22, 9 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l21" >Line 21:</td>
<td colspan="2" class="diff-lineno">Line 21:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding <ins class="diffchange diffchange-inline">(Figure 1)</ins>, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|300px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[File:pkd-cbm44.png|thumb|300px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</div></td></tr>
</table>
Marie-Katherin Zuehlke
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_44&diff=16997&oldid=prev
Marie-Katherin Zuehlke at 16:21, 9 January 2023
2023-01-09T16:21:05Z
<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:21, 9 January 2023</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l22" >Line 22:</td>
<td colspan="2" class="diff-lineno">Line 22:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Structural Features ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Like many CBMs, CBM44 exhibits a typical ß-sandwich fold: two antiparallel ß-sheets form a concave and a convex surface. The concave surface forms a deep hydrophobic ligand-binding cleft that is estimated to accommodate up to five glucose residues (~24 Å). Here, three tryptophans (W189, W194 and W198) act as key residues to mediate ligand binding, as confirmed by affinity gel electrophoresis (AGE) and ITC analyses of specific mutants <cite>Najmudin2006</cite>. The orientation of the tryptophans corresponds to the slightly twisted conformation of cello-oligosaccharides in solution <cite>Sugiyama2000</cite>. </div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">[[File:pkd-cbm44.png|thumb|300px|right|'''Figure 1.''' Three-dimensional structure of PKD-CBM44 as two domains of the multimodular cellulase ''Ct''Cel9D-Cel44A from ''Acetivibrio thermocellus'' ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>. The PKD domain is shown in orange, CBM44 in purple. The tryptophans involved in ligand recognition are highlighted. The calcium atoms of both modules are shown as red spheres.]]</ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Functionalities == </div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l27" >Line 27:</td>
<td colspan="2" class="diff-lineno">Line 29:</td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Family Firsts ==</div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase <del class="diffchange diffchange-inline">CtCel9D</del>-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>;First Identified: CBM44 was first described as an unknown C-terminal domain in the multimodular cellulase <ins class="diffchange diffchange-inline">''Ct''Cel9D</ins>-Cel44A in ''Acetivibrio thermocellus'', formerly designated as CelJ and as ''Clostridium thermocellum'' <cite>#Ahsan1996 #Arai2003</cite>. The protein also features two catalytic domains ([[GH44]] and [[GH9]]), a [[CBM30]] and an internal dockerin to target the protein to the cellulosome. The C-terminal region was then identified as having a PKD module as well as a novel CBM binding ß-1,4-glucans, hereby founding the family 44 <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>;First Structural Characterization: The same CBM44, together with the preceding PKD module, represents the first structurally characterized candidate of this family ([https://www.rcsb.org/structure/2c26 PDB 2C26]) <cite>Najmudin2006</cite>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"></td></tr>
</table>
Marie-Katherin Zuehlke