2E4T

Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum

2E4T の概要

• エントリーDOI: 10.2210/pdb2e4t/pdb
• 関連するPDBエントリー: 2E0P
• 分子名称: Endoglucanase, ZINC ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: tim barrel, tim-like barrel, composite domain of glycosyl hydrolase families 5, 30, 39 and 51, hydrolase
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58197.83

構造登録者

Kitago, Y.,Karita, S.,Watanabe, N.,Sakka, K.,Tanaka, I. (登録日: 2006-12-16, 公開日: 2007-09-18, 最終更新日: 2024-03-13)

主引用文献

Kitago, Y.,Karita, S.,Watanabe, N.,Kamiya, M.,Aizawa, T.,Sakka, K.,Tanaka, I.
Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum.
J.Biol.Chem., 282:35703-35711, 2007

PubMed Abstract: The crystal structure of Cel44A, which is one of the enzymatic components of the cellulosome of Clostridium thermocellum, was solved at a resolution of 0.96 A. This enzyme belongs to glycoside hydrolase family (GH family) 44. The structure reveals that Cel44A consists of a TIM-like barrel domain and a beta-sandwich domain. The wild-type and the E186Q mutant structures complexed with substrates suggest that two glutamic acid residues, Glu(186) and Glu(359), are the active residues of the enzyme. Biochemical experiments were performed to confirm this idea. The structural features indicate that GH family 44 belongs to clan GH-A and that the reaction catalyzed by Cel44A is retaining type hydrolysis. The stereochemical course of hydrolysis was confirmed by a (1)H NMR experiment using the reduced cellooligosaccharide as a substrate.

PubMed: 17905739
DOI: 10.1074/jbc.M706835200

実験手法

X-RAY DIFFRACTION (0.96 Å)