Abstract
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.
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