Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium.
The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-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 (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.
Nijikken
Yuri
Y
Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.
Tsukada
Takeshi
T
Igarashi
Kiyohiko
K
Samejima
Masahiro
M
Wakagi
Takayoshi
T
Shoun
Hirofumi
H
Fushinobu
Shinya
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D002850:Chromatography, Gel; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry*; D005942:Gluconates / Q000737:chemistry; D007783:Lactones; D008969:Molecular Sequence Data; D020075:Phanerochaete / Q000201:enzymology*; D011487:Protein Conformation; D001617:beta-Glucosidase / Q000737:chemistry*
D005656:Fungal Proteins; D005942:Gluconates; D007783:Lactones; D001617:beta-Glucosidase; C010730:beta-glucono-1,5-lactone