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Crystal structure of intracellular family 1 β‐glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium
Author(s) -
Nijikken Yuri,
Tsukada Takeshi,
Igarashi Kiyohiko,
Samejima Masahiro,
Wakagi Takayoshi,
Shoun Hirofumi,
Fushinobu Shinya
Publication year - 2007
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.2007.03.009
Subject(s) - phanerochaete , chrysosporium , cellobiose , glycoside hydrolase , chemistry , hydrolase , stereochemistry , intracellular , hydrolysis , active site , enzyme , biochemistry , cellulase
The white‐rot fungus Phanerochaete chrysosporium has two intracellular β‐glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate‐free and gluconolactone complexed forms. The overall structure and the characteristic of subsite −1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (β/α) 8 barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.