https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&feed=atom&action=history
Carbohydrate Binding Module Family 71 - Revision history
2024-03-28T22:31:49Z
Revision history for this page on the wiki
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Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"
2021-12-18T21:14:47Z
<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>Ben Pluvinage<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>Ben Pluvinage<ins class="diffchange diffchange-inline">|Ben Pluvinage]]</ins></div></td></tr>
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Harry Brumer
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=14404&oldid=prev
Ben Pluvinage at 17:14, 13 December 2019
2019-12-13T17:14:04Z
<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;"></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:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]</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:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1 <ins class="diffchange diffchange-inline">([{{PDBlink}}4CUB 4CUB])</ins>. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]</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>The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).</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 CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l26" >Line 26:</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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pi interactions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site <cite>Singh2014</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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pi interactions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site <cite>Singh2014</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site <ins class="diffchange diffchange-inline">([{{PDBlink}}4CUB 4CUB])</ins>. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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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Ben Pluvinage
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=14403&oldid=prev
Al Boraston at 16:55, 13 December 2019
2019-12-13T16:55:55Z
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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>{{<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]]: ^^^Ben Pluvinage^^^</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]]: ^^^Ben Pluvinage^^^</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]]: ^^^Al Boraston^^^</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]]: ^^^Al Boraston^^^</div></td></tr>
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Al Boraston
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=14387&oldid=prev
Elizabeth Ficko-Blean at 15:04, 11 December 2019
2019-12-11T15:04:00Z
<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>The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''<cite>Singh2014</cite>. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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 CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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>
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Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=14386&oldid=prev
Elizabeth Ficko-Blean at 15:03, 11 December 2019
2019-12-11T15:03:32Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 15:03, 11 December 2019</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;"></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>The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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 CBM71-1 <ins class="diffchange diffchange-inline"><cite>Singh2014</cite> </ins>solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pi interactions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pi interactions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site <ins class="diffchange diffchange-inline"><cite>Singh2014</cite></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>[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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>The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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 CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''<ins class="diffchange diffchange-inline"><cite>Singh2014</cite></ins>. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=14385&oldid=prev
Elizabeth Ficko-Blean at 14:59, 11 December 2019
2019-12-11T14:59:23Z
<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 14:59, 11 December 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l24" >Line 24:</td>
<td colspan="2" class="diff-lineno">Line 24:</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>The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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 CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s type C <del class="diffchange diffchange-inline">CBM </del><cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-<del class="diffchange diffchange-inline">pinteractions </del>with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s <ins class="diffchange diffchange-inline">[[Carbohydrate-binding_modules#Types|</ins>type C<ins class="diffchange diffchange-inline">]] CBMs </ins><cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-<ins class="diffchange diffchange-inline">pi interactions </ins>with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</div></td></tr>
<tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l32" >Line 32:</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</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<ins class="diffchange diffchange-inline">: </ins>The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.</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 CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.</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<ins class="diffchange diffchange-inline">: </ins>The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014. </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</div></td><td colspan="2"> </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 first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014. </div></td><td colspan="2"> </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>
</table>
Elizabeth Ficko-Blean
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=13658&oldid=prev
Ben Pluvinage at 22:41, 10 April 2019
2019-04-10T22:41:02Z
<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 22:41, 10 April 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</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>== 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>The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized <del class="diffchange diffchange-inline">in parallel </del>with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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 CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized <ins class="diffchange diffchange-inline">along </ins>with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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>
Ben Pluvinage
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=13657&oldid=prev
Ben Pluvinage at 22:40, 10 April 2019
2019-04-10T22:40:16Z
<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 22:40, 10 April 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l29" >Line 29:</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>== 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>The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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 CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''<ins class="diffchange diffchange-inline">. </ins> BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</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>
Ben Pluvinage
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=13656&oldid=prev
Ben Pluvinage at 22:39, 10 April 2019
2019-04-10T22:39:34Z
<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 22:39, 10 April 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l24" >Line 24:</td>
<td colspan="2" class="diff-lineno">Line 24:</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>The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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 CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making <del class="diffchange diffchange-inline">CBM71 a </del>type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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>binding site located at the apex of the β-fold opposite the N- and C-termini, making <ins class="diffchange diffchange-inline">CBM71s </ins>type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</div></td></tr>
</table>
Ben Pluvinage
https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_71&diff=13655&oldid=prev
Ben Pluvinage at 22:38, 10 April 2019
2019-04-10T22:38:54Z
<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 22:38, 10 April 2019</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l24" >Line 24:</td>
<td colspan="2" class="diff-lineno">Line 24:</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>The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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 CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow </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>binding site located at the apex of the β-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site<del class="diffchange diffchange-inline">. Therefore, the CBM71 family can be classified as type C CBM <cite>Boraston2004</cite></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>binding site located at the apex of the β-fold opposite the N- and C-termini<ins class="diffchange diffchange-inline">, making CBM71 a type C CBM <cite>Boraston2004</cite></ins>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. </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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</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:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]</div></td></tr>
</table>
Ben Pluvinage