https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_49&feed=atom&action=historyCarbohydrate Binding Module Family 49 - Revision history2024-03-29T14:32:49ZRevision history for this page on the wikiMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_49&diff=16698&oldid=prevHarry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"2021-12-18T21:20:50Z<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>Breeanna Urbanowicz<del class="diffchange diffchange-inline">^^^ </del>and <del class="diffchange diffchange-inline">^^^</del>Elizabeth Ficko-Blean<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:Breeanna Urbanowicz|</ins>Breeanna Urbanowicz<ins class="diffchange diffchange-inline">]] </ins>and <ins class="diffchange diffchange-inline">[[User:</ins>Elizabeth Ficko-Blean<ins class="diffchange diffchange-inline">|Elizabeth Ficko-Blean]]</ins></div></td></tr>
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</table>Harry Brumerhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_49&diff=13434&oldid=prevElizabeth Ficko-Blean: /* Functionalities */2018-11-23T09:19:20Z<p><span dir="auto"><span class="autocomment">Functionalities</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:19, 23 November 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l25" >Line 25:</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> </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>
<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>CBM49 modules are found appended to plant GH9 endoglucanases, and are described as unique to plants <cite>Urbanowicz2007</cite> though [http://www.cazy.org/CBM49_all.html CAZy] has also classified proteins from Amoebozoa into the CBM49 family. The three members of plant [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9 class C]] have not been well studied in ''Arabidopsis'', however, the tomato and rice orthologs of At1g64390 (AtGH9C2) have been examined. For example, Urbanowicz et al. provided evidence for the binding of the tomato SlCel9C1 CBM to crystalline cellulose, as well as hydrolysis of artificial cellulosic polymers and a variety of plant cell wall polysaccharides by the catalytic domain <cite>Urbanowicz2007a</cite>. A similar study was performed on the orthologous rice endoglucanase by Yoshida and Komae , further confirming that the catalytic domain is capable of hydrolyzing a suite of polysaccharides <cite>Yoshida2006b</cite>. There is also evidence that the rice CBM49 (previously called a CBM2) is post-translationally cleaved from a 67 kDa form to 51 kDa endoglucanase isoforms <cite>Yoshida2006a</cite>. The authors suggest this may play a role in establishment of lateral root primordia from differentiated pericycle cells as the CBM likely facilitates the hydrolysis of crystalline cellulose <cite>Yoshida2006a</cite>. Thus, the uncleaved enzyme could participate in the removal of secondary walls from the pericycle cells which contain crystalline and insoluble polymers <cite>Yoshida2006a</cite>. The authors also suggest another alternative, that the full-length enzyme may be inactive until it reaches its target in the cell wall, where it is then cleaved by proteolysis so that the catalytic domain is 'activated' in proximity to the substrate <cite>Yoshida2006a</cite>. Glass et al. have shown that over-expression of poplar PtGH9C2 in ''Arabidopsis'' together with down-regulation of ''Arabidopsis'' AtGH9C2 using RNAi, results in plants with modified degrees of cell wall crystallinity, which was inversely correlated with changes in plant height and rosette diameter <cite>Glass2015</cite>. Thus, over-expression of PtGH9C2 resulted in a decrease in height and rosette diameter and an increase in cell wall crystallinity <cite>Glass2015</cite>. Whereas downregulating AtGH9C2 increased height and rosette diameter and decreased cell wall crystallinity <cite>Glass2015</cite>. The authors suggest that genetic modification of PtGH9C2 and AtGH9C2 expression levels ''in planta'' indicate that their CBM49s function to target the GH9 enzymes to crystalline cellulose prior to proteolytic cleavage, thereby regulating cross-linking with hemicellulosic polysaccharides, preserving the crystallinity of the newly synthesized cellulose microfibrils and limiting cell expansion <cite>Glass2015, Fujita2011, Lai-Kee-Him2002, McQueen-Mason1995</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>CBM49 modules are found appended to plant GH9 endoglucanases, and are described as unique to plants <cite>Urbanowicz2007</cite> though [http://www.cazy.org/CBM49_all.html CAZy] has also classified proteins from Amoebozoa into the CBM49 family. The three members of plant [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9 class C]] have not been well studied in ''Arabidopsis'', however, the tomato and rice orthologs of At1g64390 (AtGH9C2) have been examined. For example, Urbanowicz et al. provided evidence for the binding of the tomato SlCel9C1 CBM to crystalline cellulose, as well as hydrolysis of artificial cellulosic polymers and a variety of plant cell wall polysaccharides by the catalytic domain <cite>Urbanowicz2007a</cite>. A similar study was performed on the orthologous rice endoglucanase by Yoshida and Komae , further confirming that the catalytic domain is capable of hydrolyzing a suite of polysaccharides <cite>Yoshida2006b</cite>. There is also evidence that the rice CBM49 (previously called a CBM2) is post-translationally cleaved from a 67 kDa form to 51 kDa endoglucanase isoforms <cite>Yoshida2006a</cite>. The authors suggest this may play a role in establishment of lateral root primordia from differentiated pericycle cells as the CBM likely facilitates the hydrolysis of crystalline cellulose <cite>Yoshida2006a</cite>. Thus, the uncleaved enzyme could participate in the removal of secondary walls from the pericycle cells which contain crystalline and insoluble polymers <cite>Yoshida2006a</cite>. The authors also suggest another alternative, that the full-length enzyme may be inactive until it reaches its target in the cell wall, where it is then cleaved by proteolysis so that the catalytic domain is 'activated' in proximity to the substrate <cite>Yoshida2006a</cite>. Glass et al. have shown that over-expression of poplar PtGH9C2 in ''Arabidopsis''<ins class="diffchange diffchange-inline">, </ins>together with down-regulation of ''Arabidopsis'' AtGH9C2 using RNAi, results in plants with modified degrees of cell wall crystallinity, which was inversely correlated with changes in plant height and rosette diameter <cite>Glass2015</cite>. Thus, over-expression of PtGH9C2 resulted in a decrease in height and rosette diameter and an increase in cell wall crystallinity <cite>Glass2015</cite>. Whereas downregulating AtGH9C2 increased height and rosette diameter and decreased cell wall crystallinity <cite>Glass2015</cite>. The authors suggest that genetic modification of PtGH9C2 and AtGH9C2 expression levels ''in planta'' indicate that their CBM49s function to target the GH9 enzymes to crystalline cellulose prior to proteolytic cleavage, thereby regulating cross-linking with hemicellulosic polysaccharides, preserving the crystallinity of the newly synthesized cellulose microfibrils and limiting cell expansion <cite>Glass2015, Fujita2011, Lai-Kee-Him2002, McQueen-Mason1995</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_49&diff=13433&oldid=prevElizabeth Ficko-Blean: /* Functionalities */2018-11-23T09:18:54Z<p><span dir="auto"><span class="autocomment">Functionalities</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:18, 23 November 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> </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>
<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>CBM49 modules are found appended to plant GH9 endoglucanases, and are described as unique to plants <cite>Urbanowicz2007</cite> though [http://www.cazy.org/CBM49_all.html CAZy] has also classified proteins from Amoebozoa into the CBM49 family. The three members of plant [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9 class C]] have not been well studied in ''Arabidopsis'', however, the tomato and rice orthologs of At1g64390 (AtGH9C2) have been examined. For example, Urbanowicz et al. provided evidence for the binding of the tomato SlCel9C1 CBM to crystalline cellulose, as well as hydrolysis of artificial cellulosic polymers and a variety of plant cell wall polysaccharides by the catalytic domain <cite>Urbanowicz2007a</cite>. A similar study was performed on the orthologous rice endoglucanase by Yoshida and Komae , further confirming that the catalytic domain is capable of hydrolyzing a suite of polysaccharides <cite>Yoshida2006b</cite>. There is also evidence that the rice CBM49 (previously called a CBM2) is post-translationally cleaved from a 67 kDa form to 51 kDa endoglucanase isoforms <cite>Yoshida2006a</cite>. The authors suggest this may play a role in establishment of lateral root primordia from differentiated pericycle cells as the CBM likely facilitates the hydrolysis of crystalline cellulose <cite>Yoshida2006a</cite>. Thus, the uncleaved enzyme could participate in the removal of secondary walls from the pericycle cells which contain crystalline and insoluble polymers <cite>Yoshida2006a</cite>. The authors also suggest another alternative, that the full-length enzyme may be inactive until it reaches its target in the cell wall, where it is then cleaved by proteolysis so that the catalytic domain is 'activated' in proximity to the substrate <cite>Yoshida2006a</cite>. Glass et al. have shown that over-expression of poplar PtGH9C2 in ''Arabidopsis'' together with down-regulation of ''Arabidopsis'' AtGH9C2 using RNAi results in plants with modified degrees of cell wall crystallinity, which was inversely correlated with changes in plant height and rosette diameter <cite>Glass2015</cite>. Thus, over-expression of PtGH9C2 resulted in a decrease in height and rosette diameter and an increase in cell wall crystallinity <cite>Glass2015</cite>. Whereas downregulating AtGH9C2 increased height and rosette diameter and decreased cell wall crystallinity <cite>Glass2015</cite>. The authors suggest that genetic modification of PtGH9C2 and AtGH9C2 expression levels ''in planta'' indicate that their CBM49s function to target the GH9 enzymes to crystalline cellulose prior to proteolytic cleavage, thereby regulating cross-linking with hemicellulosic polysaccharides, preserving the crystallinity of the newly synthesized cellulose microfibrils and limiting cell expansion <cite>Glass2015, Fujita2011, Lai-Kee-Him2002, McQueen-Mason1995</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>CBM49 modules are found appended to plant GH9 endoglucanases, and are described as unique to plants <cite>Urbanowicz2007</cite> though [http://www.cazy.org/CBM49_all.html CAZy] has also classified proteins from Amoebozoa into the CBM49 family. The three members of plant [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9 class C]] have not been well studied in ''Arabidopsis'', however, the tomato and rice orthologs of At1g64390 (AtGH9C2) have been examined. For example, Urbanowicz et al. provided evidence for the binding of the tomato SlCel9C1 CBM to crystalline cellulose, as well as hydrolysis of artificial cellulosic polymers and a variety of plant cell wall polysaccharides by the catalytic domain <cite>Urbanowicz2007a</cite>. A similar study was performed on the orthologous rice endoglucanase by Yoshida and Komae , further confirming that the catalytic domain is capable of hydrolyzing a suite of polysaccharides <cite>Yoshida2006b</cite>. There is also evidence that the rice CBM49 (previously called a CBM2) is post-translationally cleaved from a 67 kDa form to 51 kDa endoglucanase isoforms <cite>Yoshida2006a</cite>. The authors suggest this may play a role in establishment of lateral root primordia from differentiated pericycle cells as the CBM likely facilitates the hydrolysis of crystalline cellulose <cite>Yoshida2006a</cite>. Thus, the uncleaved enzyme could participate in the removal of secondary walls from the pericycle cells which contain crystalline and insoluble polymers <cite>Yoshida2006a</cite>. The authors also suggest another alternative, that the full-length enzyme may be inactive until it reaches its target in the cell wall, where it is then cleaved by proteolysis so that the catalytic domain is 'activated' in proximity to the substrate <cite>Yoshida2006a</cite>. Glass et al. have shown that over-expression of poplar PtGH9C2 in ''Arabidopsis'' together with down-regulation of ''Arabidopsis'' AtGH9C2 using RNAi<ins class="diffchange diffchange-inline">, </ins>results in plants with modified degrees of cell wall crystallinity, which was inversely correlated with changes in plant height and rosette diameter <cite>Glass2015</cite>. Thus, over-expression of PtGH9C2 resulted in a decrease in height and rosette diameter and an increase in cell wall crystallinity <cite>Glass2015</cite>. Whereas downregulating AtGH9C2 increased height and rosette diameter and decreased cell wall crystallinity <cite>Glass2015</cite>. The authors suggest that genetic modification of PtGH9C2 and AtGH9C2 expression levels ''in planta'' indicate that their CBM49s function to target the GH9 enzymes to crystalline cellulose prior to proteolytic cleavage, thereby regulating cross-linking with hemicellulosic polysaccharides, preserving the crystallinity of the newly synthesized cellulose microfibrils and limiting cell expansion <cite>Glass2015, Fujita2011, Lai-Kee-Him2002, McQueen-Mason1995</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_49&diff=13422&oldid=prevBreeanna Urbanowicz at 21:37, 16 November 20182018-11-16T21:37:40Z<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><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --></div></td></tr>
<tr><td class='diff-marker'>−</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>{{<del class="diffchange diffchange-inline">UnderConstruction</del>}}</div></td><td class='diff-marker'>+</td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>{{<ins class="diffchange diffchange-inline">CuratorApproved</ins>}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Breeanna Urbanowicz^^^ and ^^^Elizabeth Ficko-Blean^^^</div></td><td class='diff-marker'> </td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[Author]]: ^^^Breeanna Urbanowicz^^^ and ^^^Elizabeth Ficko-Blean^^^</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]]: ^^^Breeanna Urbanowicz^^^</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]]: ^^^Breeanna Urbanowicz^^^</div></td></tr>
</table>Breeanna Urbanowiczhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_49&diff=13263&oldid=prevElizabeth Ficko-Blean at 15:10, 28 August 20182018-08-28T15:10:03Z<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 15:10, 28 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l19" >Line 19:</td>
<td colspan="2" class="diff-lineno">Line 19:</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM <del class="diffchange diffchange-inline">showing </del>the proposed functionally important residues <del class="diffchange diffchange-inline">is </del>shown in <del class="diffchange diffchange-inline">cyan</del>. The [[CBM2]] NMR template<del class="diffchange diffchange-inline">, </del>used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG])<del class="diffchange diffchange-inline">, </del>is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM <ins class="diffchange diffchange-inline">is shown in cyan, </ins>the proposed functionally important residues <ins class="diffchange diffchange-inline">are </ins>shown in <ins class="diffchange diffchange-inline">stick</ins>. The [[CBM2]] NMR template used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]) is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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_49&diff=13262&oldid=prevElizabeth Ficko-Blean at 15:06, 28 August 20182018-08-28T15:06:57Z<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 15:06, 28 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l19" >Line 19:</td>
<td colspan="2" class="diff-lineno">Line 19:</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM showing the proposed functionally important residues is shown in cyan. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</cite>]]<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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM showing the proposed functionally important residues is shown in cyan. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</cite><ins class="diffchange diffchange-inline">.</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>== 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_49&diff=13252&oldid=prevElizabeth Ficko-Blean at 11:43, 28 August 20182018-08-28T11:43:01Z<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 11:43, 28 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l19" >Line 19:</td>
<td colspan="2" class="diff-lineno">Line 19:</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM showing the proposed functionally important residues is shown in cyan. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM showing the proposed functionally important residues is shown in cyan. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</cite>]]<ins class="diffchange diffchange-inline">.</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>== 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_49&diff=13251&oldid=prevElizabeth Ficko-Blean at 10:07, 28 August 20182018-08-28T10:07:17Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en-CA">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 10:07, 28 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l19" >Line 19:</td>
<td colspan="2" class="diff-lineno">Line 19:</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] ([[GH9]]), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM <del class="diffchange diffchange-inline">(cyan) </del>showing the proposed functionally important residues. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM showing the proposed functionally important residues <ins class="diffchange diffchange-inline">is shown in cyan</ins>. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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_49&diff=13250&oldid=prevElizabeth Ficko-Blean at 09:57, 28 August 20182018-08-28T09:57:05Z<p></p>
<table class="diff diff-contentalign-left diff-editfont-monospace" data-mw="interface">
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<col class="diff-content" />
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<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 09:57, 28 August 2018</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l17" >Line 17:</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] (GH9), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|Plant endoglucanases]] belong to [[Glycoside Hydrolase Family 9]] (<ins class="diffchange diffchange-inline">[[</ins>GH9<ins class="diffchange diffchange-inline">]]</ins>), which contains enzymes capable of hydrolysing β-1,4 glycosidic bonds within a glycan chain. The [[GH9]] family in plants has been divided into three sub-families on the basis of variations in protein sequences <cite>Urbanowicz2007b, Libertini2004</cite>. The [[Glycoside_Hydrolase_Family_9/Plant_endoglucanases|GH9C]] sub-family proteins are comprised of a single N-terminal transmembrane helix, a [[GH9]] catalytic domain, and a C-terminal carbohydrate binding module (CBM49). Urbanowicz et al. showed that the CBM49 module of SlCel9C1 from ''Solanum lycopersicum'' binds crystalline cellulose <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM (cyan) showing the proposed functionally important residues. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</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>[[Image:Structure-CBM49.jpg|thumb|300px|right|'''Figure 1.''' A secondary structure representation of the predicted model of SlCel9C1 CBM (cyan) showing the proposed functionally important residues. The [[CBM2]] NMR template, used for model prediction (PDB ID [{{PDBlink}}1exg 1EXG]), is shown in red. This figure was adapted from <cite>Urbanowicz2007a</cite>]]</div></td></tr>
</table>Elizabeth Ficko-Bleanhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_49&diff=13249&oldid=prevElizabeth Ficko-Blean at 09:56, 28 August 20182018-08-28T09:56:21Z<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 09:56, 28 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;"></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>CBM49 domains are about 100–110 amino acids long <cite>Urbanowicz2007a</cite>. BLAST searches and predictive protein modeling indicate that these domains are most similar to CBM2 <cite>Urbanowicz2007a</cite>. A refined model of the SlCel9C1 CBM domain, based on the [[Carbohydrate-binding_modules#Types|type A]]-binding [[CBM2]] NMR template from ''Cellulomonas fimi'' xylanase 10A (PDB ID [{{PDBlink}}1exg 1EXG]), closely matched the features of the β-barrel fold of the parent structure (i.e. only a few short insertions/deletions are present in the final alignment) <cite>Urbanowicz2007a</cite>. The model indicates surface localization of three key tryptophan residues, Trp522, Trp559, and Trp573 on the predicted β-barrel fold <cite>Urbanowicz2007a</cite>. Furthermore, site-directed mutagenesis of SlCel9C1-CBM49 showed that Trp522, Trp559, and Trp573 contribute to the interaction of the CBM49 module with crystalline cellulose (BMCC) <cite>Urbanowicz2007a</cite>. These results suggest that the CBM49 interacts through a [[Carbohydrate-binding_modules#Types|type A]] mechanism. </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>CBM49 domains are about 100–110 amino acids long <cite>Urbanowicz2007a</cite>. BLAST searches and predictive protein modeling indicate that these domains are most similar to CBM2 <cite>Urbanowicz2007a</cite>. A refined model of the SlCel9C1 CBM domain <ins class="diffchange diffchange-inline">(Figure 1)</ins>, based on the [[Carbohydrate-binding_modules#Types|type A]]-binding [[CBM2]] NMR template from ''Cellulomonas fimi'' xylanase 10A (PDB ID [{{PDBlink}}1exg 1EXG]), closely matched the features of the β-barrel fold of the parent structure (i.e. only a few short insertions/deletions are present in the final alignment) <cite>Urbanowicz2007a</cite>. The model indicates surface localization of three key tryptophan residues, Trp522, Trp559, and Trp573 on the predicted β-barrel fold <cite>Urbanowicz2007a</cite>. Furthermore, site-directed mutagenesis of SlCel9C1-CBM49 showed that Trp522, Trp559, and Trp573 contribute to the interaction of the CBM49 module with crystalline cellulose (BMCC) <cite>Urbanowicz2007a</cite>. These results suggest that the CBM49 interacts through a [[Carbohydrate-binding_modules#Types|type A]] mechanism. </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>
<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