4c4c

Michaelis complex of Hypocrea jecorina CEL7A E217Q mutant with cellononaose spanning the active site

spinqualitylabelsall models 4c4c, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c4c is a 1 chain structure with sequence from Atcc 13631. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, CO, NAG, PEG NonStd Res: PCA Related: 4c4d Activity: Cellulose 1,4-beta-cellobiosidase (non-reducing end), with EC number 3.2.1.91 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GUX1_HYPJE] 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. Publication Abstract from PubMed Glycoside hydrolases (GHs) cleave glycosidic linkages in carbohydrates, typically via inverting or retaining mechanisms, the latter of which proceeds via a two-step mechanism that includes formation of a glycosyl-enzyme intermediate. We present two new structures of the catalytic domain of Hypocrea jecorina GH Family 7 cellobiohydrolase Cel7A, namely a Michaelis complex with a full cellononaose ligand and a glycosyl-enzyme intermediate, that reveal details of the 'static' reaction coordinate. We also employ transition path sampling to determine the 'dynamic' reaction coordinate for the catalytic cycle. The glycosylation reaction coordinate contains components of forming and breaking bonds and a conformational change in the nucleophile. Deglycosylation proceeds via a product-assisted mechanism wherein the glycosylation product, cellobiose, positions a water molecule for nucleophilic attack on the anomeric carbon of the glycosyl-enzyme intermediate. In concert with previous structures, the present results reveal the complete hydrolytic reaction coordinate for this naturally and industrially important enzyme family. The Mechanism of Cellulose Hydrolysis by a Two-Step, Retaining Cellobiohydrolase Elucidated by Structural and Transition Path Sampling Studies.,Knott BC, Haddad Momeni M, Crowley MF, Mackenzie LF, Gotz AW, Sandgren M, Withers SG, Stahlberg J, Beckham GT J Am Chem Soc. 2013 Dec 16. PMID:24341799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellobiohydrolase 3D structures

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