https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&feed=atom&action=historyCarbohydrate Binding Module Family 79 - Revision history2024-03-28T21:15:04ZRevision history for this page on the wikiMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=16660&oldid=prevHarry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"2021-12-18T21:19:31Z<p>Text replacement - "\^\^\^(.*)\^\^\^" to "<a href="/index.php?title=User:$1&action=edit&redlink=1" class="new" title="User:$1 (page does not exist)">$1</a>"</p>
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<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>* [[Author]]: <del class="diffchange diffchange-inline">^^^</del>Immacolata Venditto<del class="diffchange diffchange-inline">^^^</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>* [[Author]]: <ins class="diffchange diffchange-inline">[[User:</ins>Immacolata Venditto<ins class="diffchange diffchange-inline">|Immacolata Venditto]]</ins></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>* [[Responsible Curator]]: <del class="diffchange diffchange-inline">^^^</del>Harry Gilbert<del class="diffchange diffchange-inline">^^^</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>* [[Responsible Curator]]: <ins class="diffchange diffchange-inline">[[User:</ins>Harry Gilbert<ins class="diffchange diffchange-inline">|Harry Gilbert]]</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>----</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>----</div></td></tr>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13284&oldid=prevElizabeth Ficko-Blean at 08:59, 30 August 20182018-08-30T08:59:22Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:59, 30 August 2018</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>* [[Author]]: ^^^Immacolata Venditto^^^</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]]: ^^^Immacolata Venditto^^^</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]]: ^^^Harry Gilbert^^^</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]]: ^^^Harry Gilbert^^^</div></td></tr>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13283&oldid=prevHarry Brumer at 18:22, 29 August 20182018-08-29T18:22:36Z<p></p>
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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>== 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>[[File:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L]<del class="diffchange diffchange-inline">)(</del>[{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L]<ins class="diffchange diffchange-inline">, </ins>[{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft/planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]. Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft/planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]. Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</cite>.</div></td></tr>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13281&oldid=prevElizabeth Ficko-Blean at 09:49, 29 August 20182018-08-29T09:49:47Z<p></p>
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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>== 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 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>CBM79 fulfills an enzyme-targeting role that is specific to ''Ruminococcus'' <cite>Bensoussan2017</cite>. ''R. flavefaciens'' forms a multi-enzyme cellulosome complex that plays an integral role in the ability of this bacterium to degrade plant cell wall polysaccharides <cite>BergMiller2009</cite>. CBMs generally display specificities consistent with the activity of the appended enzyme. ''R. flavefaciens'' CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub> are components of an enzyme that contains a [[GH9]] catalytic module <cite>VendittoI2016</cite>. The specificity of CBM79-1<sub>RfGH9</sub> for β-glucans is consistent with endo-β1,4-glucanase activity of the [[GH9]] catalytic module <cite>VendittoI2016</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>CBM79 fulfills an enzyme-targeting role that is specific to ''Ruminococcus'' <cite>Bensoussan2017</cite>. ''R. flavefaciens'' forms a multi-enzyme cellulosome complex that plays an integral role in the ability of this bacterium to degrade plant cell wall polysaccharides <cite>BergMiller2009</cite>. CBMs generally display specificities consistent with the activity of the appended enzyme. ''R. flavefaciens'' CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub> are components of an enzyme that contains a [[GH9]] catalytic module <cite>VendittoI2016</cite>. The specificity of CBM79-1<sub>RfGH9</sub> for β-glucans is consistent with <ins class="diffchange diffchange-inline">targeting the </ins>endo-β1,4-glucanase activity of the [[GH9]] catalytic module <ins class="diffchange diffchange-inline">to its substrate </ins><cite>VendittoI2016</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>== 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>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13280&oldid=prevElizabeth Ficko-Blean at 09:48, 29 August 20182018-08-29T09:48:19Z<p></p>
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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>== 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="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>''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (<del class="diffchange diffchange-inline">noncrystalline</del>) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants Trp564A and Trp607A retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of Trp564 and Trp606 resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (<ins class="diffchange diffchange-inline">non-crystalline</ins>) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants Trp564A and Trp607A retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of Trp564 and Trp606 resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13279&oldid=prevElizabeth Ficko-Blean at 09:35, 29 August 20182018-08-29T09:35:13Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:35, 29 August 2018</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><del class="diffchange diffchange-inline">CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. </del>''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. <ins class="diffchange diffchange-inline">CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. </ins>Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (noncrystalline) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants Trp564A and Trp607A retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of Trp564 and Trp606 resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (noncrystalline) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants Trp564A and Trp607A retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of Trp564 and Trp606 resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13278&oldid=prevElizabeth Ficko-Blean at 09:33, 29 August 20182018-08-29T09:33:59Z<p></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 09:33, 29 August 2018</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>== 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="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>CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. ''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>CBM79 is a family identified in the ''Ruminococcus flavefaciens'' cellulosome. ''Ruminococcus flavefaciens'' is an anaerobic, cellulolytic bacterium that plays an important role in the ruminal digestion of plant cell walls <cite>RinconMT2010</cite>. Two CBM79s (CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub>) were identified in an enzyme that contains a [[GH9]] catalytic module with endo-β-1,4-glucanase activity <cite>VendittoI2016</cite>. Both CBM79s bind to a range of β-1,4- and mixed-linked β-1,3-1,4-glucans <cite>VendittoI2016</cite>. The ligand binding of CBM79-1<sub>RfGH9</sub> was quantified by Isothermal Titration Calorimetry (ITC) and semi-quantified using Microarrays <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds barley β-glucan and hydroxyethylcellulose (HEC) with similar affinities of 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. The small increase in ''K''<sub>A</sub> from cellotetraose to cellohexaose </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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (noncrystalline) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants <del class="diffchange diffchange-inline">W564A </del>and <del class="diffchange diffchange-inline">W607A </del>retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of <del class="diffchange diffchange-inline">W564 </del>and <del class="diffchange diffchange-inline">W606 </del>resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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>(''K''<sub>A</sub> 4.2 x 10<sup>3</sup> M<sup>-1</sup> for cellotetraose, ''K''<sub>A</sub> 7.0 x 10<sup>3</sup> M<sup>-1</sup> for cellopentaose and ''K''<sub>A</sub> 4.9 x 10<sup>3</sup> M<sup>-1</sup> for cellohexaose) suggests that ligand recognition is dominated by four sugar binding sites <cite>VendittoI2016</cite>. The binding to xyloglucan is weaker than the other β-glucans, indicating that the protein cannot recognize the xylose side chains <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> binds regenerated (noncrystalline) insoluble cellulose (RC) with a ''K''<sub>A</sub> of 4.8 x 10<sup>4</sup> M<sup>-1</sup> <cite>VendittoI2016</cite>. Mutagenesis experiments confirmed the importance of the aromatic residues in ligand recognition <cite>VendittoI2016</cite>. Alanine substitution of Trp606 in CBM79-1<sub>RfGH9</sub>, which is conserved in the CBM family, resulted in complete loss of binding to all ligands <cite>VendittoI2016</cite>. The mutants <ins class="diffchange diffchange-inline">Trp564A </ins>and <ins class="diffchange diffchange-inline">Trp607A </ins>retained affinity for barley β-glucan but did not bind xyloglucan <cite>VendittoI2016</cite>. Alanine substitution of <ins class="diffchange diffchange-inline">Trp564 </ins>and <ins class="diffchange diffchange-inline">Trp606 </ins>resulted in loss of binding to RC <cite>VendittoI2016</cite>. The importance of conformation of conserved aromatic residues on CBM specificity is evident in [[CBM2]] members that bind to cellulose or xylan <cite>SimpsonPJ2000</cite>. CBM79 binding to non-crystalline polysaccharides indicates that CBM79-1<sub>RfGH9</sub> is a [[Carbohydrate-binding_modules#Types|type B]] CBM <cite>VendittoI2016</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-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13277&oldid=prevElizabeth Ficko-Blean at 08:11, 29 August 20182018-08-29T08:11:16Z<p></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 08:11, 29 August 2018</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>== 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: CBM79 from the ''Ruminococcus flavefaciens'' CBM79_1<sub>RfGH9</sub> and CBM79_2<sub>RfGH9</sub> <del class="diffchange diffchange-inline"> </del><cite>VendittoI2016</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: CBM79 from the ''Ruminococcus flavefaciens'' CBM79_1<sub>RfGH9</sub> and CBM79_2<sub>RfGH9</sub> <ins class="diffchange diffchange-inline">were the first CBM79 members characterized </ins><cite>VendittoI2016</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>;First Structural Characterization: The first available crystal structure and the first complex structure of a CBM79 is from CBM79_1<sub>RfGH9</sub> <cite>VendittoI2016</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 first available crystal structure and the first complex structure of a CBM79 is from CBM79_1<sub>RfGH9</sub> <cite>VendittoI2016</cite>.</div></td></tr>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13276&oldid=prevElizabeth Ficko-Blean at 08:07, 29 August 20182018-08-29T08:07:52Z<p></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 08:07, 29 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l22" >Line 22:</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>== 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>[[File:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L])([{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L])([{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft <del class="diffchange diffchange-inline">or </del>planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]. Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft<ins class="diffchange diffchange-inline">/</ins>planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]. Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</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>== 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 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>CBM79 fulfills an enzyme-targeting role that is specific to ''Ruminococcus'' <cite>Bensoussan2017</cite>. ''R. flavefaciens'' forms a multi-enzyme cellulosome complex that plays an integral role in the ability of this bacterium to degrade plant cell wall polysaccharides <cite>BergMiller2009</cite>. CBMs generally display specificities consistent with the activity of the appended enzyme. ''R. flavefaciens'' CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub> are components of an enzyme that contains a <del class="diffchange diffchange-inline">catalytic module derived from </del>[[GH9]] <del class="diffchange diffchange-inline"> </del><cite>VendittoI2016</cite>. The specificity of CBM79-1<sub>RfGH9</sub> for β-glucans is consistent with endo-β1,4-glucanase activity of the [[GH9]] catalytic module <cite>VendittoI2016</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>CBM79 fulfills an enzyme-targeting role that is specific to ''Ruminococcus'' <cite>Bensoussan2017</cite>. ''R. flavefaciens'' forms a multi-enzyme cellulosome complex that plays an integral role in the ability of this bacterium to degrade plant cell wall polysaccharides <cite>BergMiller2009</cite>. CBMs generally display specificities consistent with the activity of the appended enzyme. ''R. flavefaciens'' CBM79-1<sub>RfGH9</sub> and CBM79-2<sub>RfGH9</sub> are components of an enzyme that contains a [[GH9]] <ins class="diffchange diffchange-inline">catalytic module </ins><cite>VendittoI2016</cite>. The specificity of CBM79-1<sub>RfGH9</sub> for β-glucans is consistent with endo-β1,4-glucanase activity of the [[GH9]] catalytic module <cite>VendittoI2016</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>== 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>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_79&diff=13275&oldid=prevElizabeth Ficko-Blean at 07:55, 29 August 20182018-08-29T07:55:28Z<p></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 07:55, 29 August 2018</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>== 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>[[File:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L])([{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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:CBM79-1.jpg|thumb|300px|right|'''Figure 1.''' Crystal structure of CBM79-1<sub>RfGH9</sub>. ([{{PDBlink}}4V1L PDB ID 4V1L])([{{PDBlink}}4V1K PDB ID 4V1K]). The aromatic residues that contribute to ligand recognition are shown.]] </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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft or planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</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>The structure of CBM79-1<sub>RfGH9</sub> was solved using single-wavelength anomalous diffraction (SAD) methods and selenomethionyl protein to a resolution of 1.8 Å <cite>VendittoI2016</cite>. CBM79-1<sub>RfGH9</sub> displays a beta-sandwich fold in which the 12 antiparallel β-strands are organized in two β-sheets 1 and 2 (Figure 1) <cite>VendittoI2016</cite>. β-sheet 2 forms a cleft in which aromatic residues are a dominant feature <cite>VendittoI2016</cite>. The ligand binding site located at the concave surface of the protein forms an unusual solvent exposed cleft or planar surface for a [[Carbohydrate-binding_modules#Types|type B]] β-glucan binding CBM. It is not a narrow canyon-like structure as displayed by [[CBM78]]<ins class="diffchange diffchange-inline">. </ins>Tyr563, Trp564, Tyr597, Trp606 and Trp607 in CBM79-1<sub>RfGH9</sub> form a twisted hydrophobic platform within the cleft <cite>VendittoI2016</cite>. Two tryptophan residues (Trp564 and Trp606) play a key role in ligand recognition adopting a planar orientation in CBM79-1<sub>RfGH9</sub> <cite>VendittoI2016</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>== 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>Elizabeth Ficko-Blean