2e40
From Proteopedia
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium in complex with gluconolactone
Overview
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.
About this Structure
2E40 is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.
Reference
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium., Nijikken Y, Tsukada T, Igarashi K, Samejima M, Wakagi T, Shoun H, Fushinobu S, FEBS Lett. 2007 Apr 3;581(7):1514-20. Epub 2007 Mar 13. PMID:17376440 Page seeded by OCA on Sun May 4 01:52:41 2008
Categories: Beta-glucosidase | Phanerochaete chrysosporium | Single protein | Fushinobu, S. | Igarashi, K. | Nijikken, Y. | Samejima, M. | Tsukada, T. | Clan gh-a | Glycoside hydrolase family 1 | National project on protein structural and functional analyse | Nppsfa | Structural genomic | Tim barrel
