1NP2

Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102

1NP2 の概要

• エントリーDOI: 10.2210/pdb1np2/pdb
• 分子名称: beta-glycosidase (2 entities in total)
• 機能のキーワード: tim barrel, hydrolase
• 由来する生物種: Thermus nonproteolyticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98112.34

構造登録者

Liang, D.C.,Chang, W.R.,Wang, X.Q.,He, X.Y. (登録日: 2003-01-16, 公開日: 2003-07-15, 最終更新日: 2023-10-25)

主引用文献

Wang, X.,He, X.,Yang, S.,An, X.,Chang, W.,Liang, D.
Structural Basis for Thermostability of beta-Glycosidase from the Thermophilic Eubacterium Thermus nonproteolyticus HG102.
J.Bacteriol., 185:4248-4255, 2003

PubMed Abstract: The three-dimensional structure of a thermostable beta-glycosidase (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 A. The core of the structure adopts the (betaalpha)(8) barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that Gly(Tn) belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of Gly(Tn) related to the thermostability and compared its structure with those of other mesophilic glycosidases from plants, eubacteria, and hyperthermophilic enzymes from archaea. Several possible features contributing to the thermostability of Gly(Tn) were elucidated.

PubMed: 12837801
DOI: 10.1128/JB.185.14.4248-4255.2003

実験手法

X-RAY DIFFRACTION (2.4 Å)