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Acta Crystallogr D Struct Biol ; 75(Pt 12): 1138-1147, 2019 Dec 01.
Article in English | MEDLINE | ID: mdl-31793907

ABSTRACT

The catalytic domain (residues 128-449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 Å, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.


Subject(s)
Bacterial Proteins/chemistry , Cellobiose/metabolism , Cellulase/chemistry , Cellulose 1,4-beta-Cellobiosidase/chemistry , Cellulose/metabolism , Neocallimastigales/enzymology , Trioses/metabolism , beta-Glucosidase/chemistry , Binding Sites , Crystallography, X-Ray/methods , Models, Molecular , Protein Conformation , Substrate Specificity
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