2E40

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

2E40 の概要

• エントリーDOI: 10.2210/pdb2e40/pdb
• 関連するPDBエントリー: 2E3Z
• 分子名称: Beta-glucosidase, D-glucono-1,5-lactone (3 entities in total)
• 機能のキーワード: tim barrel, glycoside hydrolase family 1, clan gh-a, structural genomics, nppsfa, national project on protein structural and functional analyses, hydrolase
• 由来する生物種: Phanerochaete chrysosporium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106274.30

構造登録者

Nijikken, Y.,Tsukada, T.,Igarashi, K.,Samejima, M.,Fushinobu, S. (登録日: 2006-12-01, 公開日: 2007-03-27, 最終更新日: 2023-10-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)