2E40

Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium in complex with gluconolactone

Summary for 2E40

• Entry DOI: 10.2210/pdb2e40/pdb
• Related: 2E3Z
• Descriptor: Beta-glucosidase, D-glucono-1,5-lactone (3 entities in total)
• Functional Keywords: tim barrel, glycoside hydrolase family 1, clan gh-a, structural genomics, nppsfa, national project on protein structural and functional analyses, hydrolase
• Biological source: Phanerochaete chrysosporium
• Total number of polymer chains: 2
• Total formula weight: 106274.30

Authors

Nijikken, Y.,Tsukada, T.,Igarashi, K.,Samejima, M.,Fushinobu, S. (deposition date: 2006-12-01, release date: 2007-03-27, Last modification date: 2023-10-25)

Primary citation

Nijikken, Y.,Tsukada, T.,Igarashi, K.,Samejima, M.,Wakagi, T.,Shoun, H.,Fushinobu, S.
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium
Febs Lett., 581:1514-1520, 2007

PubMed Abstract: 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.

PubMed: 17376440
DOI: 10.1016/j.febslet.2007.03.009

Experimental method

X-RAY DIFFRACTION (1.9 Å)