3abx | pdb_00003abx

CcCel6C, a glycoside hydrolase family 6 enzyme, complexed with p-nitrophenyl beta-D-cellotrioside

spinqualitylabelsall models 3abx, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3abx is a 1 chain structure with sequence from Coprinopsis cinerea. This structure supersedes the now removed PDB entry 3a9a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: MG, RCB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7X9Z2_COPCI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellobiohydrolase 3D structures

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