1G01

ALKALINE CELLULASE K CATALYTIC DOMAIN

1G01 の概要

• エントリーDOI: 10.2210/pdb1g01/pdb
• 関連するPDBエントリー: 1G0C
• 分子名称: ENDOGLUCANASE, CADMIUM ION, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha/beta barrel, tim barrel, hydrolase
• 由来する生物種: Bacillus sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41791.62

構造登録者

Shirai, T.,Ishida, H.,Noda, J.,Yamane, T.,Ozaki, K.,Hakamada, Y.,Ito, S. (登録日: 2000-10-05, 公開日: 2001-08-01, 最終更新日: 2024-03-13)

主引用文献

Shirai, T.,Ishida, H.,Noda, J.,Yamane, T.,Ozaki, K.,Hakamada, Y.,Ito, S.
Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme.
J.Mol.Biol., 310:1079-1087, 2001

PubMed Abstract: The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 A resolution. Because of the most alkaliphilic nature and it's highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.

PubMed: 11501997
DOI: 10.1006/jmbi.2001.4835

実験手法

X-RAY DIFFRACTION (1.9 Å)