4a05

Structure of the catalytic core domain of the cellobiohydrolase, Cel6A, from Chaetomium thermophilum

spinqualitylabelsall models 4a05, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a05 is a 1 chain structure with sequence from Cbs 144.50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, LI, NAG Activity: Cellulose 1,4-beta-cellobiosidase (non-reducing end), with EC number 3.2.1.91 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellobiohydrolase 3D structures

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