Premium
Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose
Author(s) -
Huang Hsiao-Chuan,
Qi Liu-Hong,
Chen Yo-Chia,
Tsai Li-Chu
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319013597
Subject(s) - cellobiose , chemistry , glycoside hydrolase , hydrolase , enzyme , stereochemistry , cellulase , active site , hydrogen bond , substrate (aquarium) , hydrolysis , molecule , biochemistry , organic chemistry , biology , ecology
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.