View source for 4a05


==Structure of the catalytic core domain of the cellobiohydrolase, Cel6A, from Chaetomium thermophilum==
<StructureSection load='4a05' size='340' side='right'caption='[[4a05]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4a05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A05 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4a05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a05 OCA], [https://pdbe.org/4a05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a05 RCSB], [https://www.ebi.ac.uk/pdbsum/4a05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a05 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0SD43_CHATD G0SD43_CHATD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cellulases, including cellobiohydrolases and endoglucanases, are important enzymes involved in the breakdown of the polysaccharide cellulose. These catalysts have found widescale industrial applications, particularly in the paper and textile industries, and are now finding use in `second-generation' conversion of biomass to biofuels. Despite this considerable biotechnological application, and undoubted future potential, uncertainty remains as to the exact reaction mechanism of the inverting cellulases found in the GH6 family of carbohydrate-active enzymes. In order to gain additional understanding as to how these societally beneficial biocatalysts function, the crystal structure of a GH6 cellobiohydrolase from Chaetomium thermophilum, CtCel6A, has been solved. This structure reveals a distorted alpha/beta-barrel fold comprising a buried tunnel-like active site quite typical of Cel6A enzymes. Analysis of an enzyme-product complex (cellobiose in the -3 and -2 subsites and cellotetraose in subsites +1 to +4) supports the hypothesis that this group of enzymes act via an atypical single-displacement mechanism. Of particular note in this analysis is an active-centre metal ion, Li(+), the position of which matches the position of the positively charged anomeric carbon of the oxocarbenium-ion-like transition state.

Structure of the catalytic core module of the Chaetomium thermophilum family GH6 cellobiohydrolase Cel6A.,Thompson AJ, Heu T, Shaghasi T, Benyamino R, Jones A, Friis EP, Wilson KS, Davies GJ Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):875-82. Epub 2012 Jul 7. PMID:22868752<ref>PMID:22868752</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4a05" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Large Structures]]
[[Category: Davies GJ]]
[[Category: Thompson AJ]]
[[Category: Wilson KS]]