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Crystal structure of the N‐terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea
Author(s) -
Miyazaki Takatsugu,
Yoshida Makoto,
Tamura Mizuki,
Tanaka Yutaro,
Umezawa Kiwamu,
Nishikawa Atsushi,
Tonozuka Takashi
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.041
Subject(s) - hydrolase , biology , glycoside hydrolase , chemistry , biochemistry , stereochemistry , enzyme
The crystal structure of the N‐terminal putative catalytic domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea (CcGH131A) was determined. The structure of CcGH131A was found to be composed of a β‐jelly roll fold and mainly consisted of two β‐sheets, sheet‐A and sheet‐B. A concave of sheet‐B, the possible active site, was wide and shallow, and three glycerol molecules were present in the concave. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues, and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases.