Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose.
Acta Crystallogr D Struct Biol
; 75(Pt 12): 1138-1147, 2019 Dec 01.
Article
em En
| 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 2.78â
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Trioses
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Celobiose
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Celulase
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Celulose
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Beta-Glucosidase
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Neocallimastigales
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Celulose 1,4-beta-Celobiosidase
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article