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==Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with sulfur substituted beta-1,4 xylopentaose.== | ==Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with sulfur substituted beta-1,4 xylopentaose.== | ||
<StructureSection load='3cuj' size='340' side='right' caption='[[3cuj]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3cuj' size='340' side='right'caption='[[3cuj]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cuj]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3cuj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUJ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900104:thio-xylopentaose'>PRD_900104</scene>, <scene name='pdbligand=TWY:(2~{R},3~{R},4~{R},5~{R})-5-sulfanyloxane-2,3,4-triol'>TWY</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuj OCA], [https://pdbe.org/3cuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cuj RCSB], [https://www.ebi.ac.uk/pdbsum/3cuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cuj ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GUX_CELFI GUX_CELFI] Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cuj_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cuj_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cuj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Glucanase|Glucanase]] | *[[Glucanase 3D structures|Glucanase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cellulomonas fimi]] | [[Category: Cellulomonas fimi]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Kuntz | [[Category: Kuntz DA]] | ||
[[Category: Rose | [[Category: Rose DR]] | ||
[[Category: Saul | [[Category: Saul M]] | ||
Latest revision as of 11:55, 30 October 2024
Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with sulfur substituted beta-1,4 xylopentaose.Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with sulfur substituted beta-1,4 xylopentaose.
Structural highlights
FunctionGUX_CELFI Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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