3abx
From Proteopedia
(Difference between revisions)
(5 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:3abx.png|left|200px]] | ||
- | + | ==CcCel6C, a glycoside hydrolase family 6 enzyme, complexed with p-nitrophenyl beta-D-cellotrioside== | |
+ | <StructureSection load='3abx' size='340' side='right'caption='[[3abx]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3abx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3a9a 3a9a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ABX FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RCB:4-NITROPHENYL+BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSIDE'>RCB</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3abx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abx OCA], [https://pdbe.org/3abx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3abx RCSB], [https://www.ebi.ac.uk/pdbsum/3abx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3abx ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/B7X9Z2_COPCI B7X9Z2_COPCI] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/3abx_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </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/main_output.php?pdb_ID=3abx ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The basidiomycete Coprinopsis cinerea produces the glycoside hydrolase family 6 enzyme CcCel6C at low and constitutive levels. CcCel6C exhibits unusual cellobiohydrolase activity; it hydrolyses carboxymethyl cellulose, which is a poor substrate for typical cellobiohydrolases. Here, we determined the crystal structures of CcCel6C unbound and in complex with p-nitrophenyl beta-D-cellotrioside and cellobiose. CcCel6C consists of a distorted seven-stranded beta/alpha barrel and has an enclosed tunnel, which is observed in other cellobiohydrolases from ascomecetes Hypocrea jecorina (HjeCel6A) and Humicola insolens (HinCel6A). In HjeCel6A and HinCel6A, ligand binding produces a conformational change that narrows this tunnel. In contrast, the tunnel remains wide in CcCel6C and the conformational change appears to be less favourable than in HjeCel6A and HinCel6A. The ligand binding cleft for subsite -3 of CcCel6C is also wide and is rather similar to that of endoglucanase. These results suggest that the open tunnel and the wide cleft are suitable for the hydrolysis of carboxymethyl cellulose. | ||
- | + | Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea.,Liu Y, Yoshida M, Kurakata Y, Miyazaki T, Igarashi K, Samejima M, Fukuda K, Nishikawa A, Tonozuka T FEBS J. 2010 Mar;277(6):1532-42. Epub 2010 Feb 10. PMID:20148970<ref>PMID:20148970</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3abx" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[Cellobiohydrolase|Cellobiohydrolase]] | + | *[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Coprinopsis cinerea]] | [[Category: Coprinopsis cinerea]] | ||
- | [[Category: Kurakata | + | [[Category: Large Structures]] |
- | [[Category: Liu | + | [[Category: Kurakata Y]] |
- | [[Category: Miyazaki | + | [[Category: Liu Y]] |
- | [[Category: Nishikawa | + | [[Category: Miyazaki T]] |
- | [[Category: Tonozuka | + | [[Category: Nishikawa A]] |
- | [[Category: Yoshida | + | [[Category: Tonozuka T]] |
- | + | [[Category: Yoshida M]] | |
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
CcCel6C, a glycoside hydrolase family 6 enzyme, complexed with p-nitrophenyl beta-D-cellotrioside
|