1LF1

Crystal Structure of Cel5 from Alkalophilic Bacillus sp.

1LF1 の概要

• エントリーDOI: 10.2210/pdb1lf1/pdb
• 分子名称: Cel5 (2 entities in total)
• 機能のキーワード: cellulose degradation, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34502.59

構造登録者

Shaw, A.,Bott, R.,Vonrhein, C.,Bricogne, G.,Power, S.,Day, A.G. (登録日: 2002-04-10, 公開日: 2002-07-03, 最終更新日: 2024-02-14)

主引用文献

Shaw, A.,Bott, R.,Vonrhein, C.,Bricogne, G.,Power, S.,Day, A.G.
A novel combination of two classic catalytic schemes.
J.Mol.Biol., 320:303-309, 2002

PubMed Abstract: The crystal structure of an alkaline Bacillus cellulase catalytic core, from glucoside hydrolase family 5, reveals a novel combination of the catalytic machinery of two classic textbook enzymes. The enzyme has the expected two glutamate residues in close proximity to one another in the active-site that are typical of retaining cellulases. However, the proton donor, glutamate 139 is also unexpectedly a member of a serine-histidine-glutamate catalytic triad, forming a novel combination of catalytic machineries. Structure and sequence analysis of glucoside hydrolase family 5 reveal that the triad is highly conserved, but with variations at the equivalent of the serine position. We speculate that the purpose of this novel catalytic triad is to control the protonation of the acid/base glutamate, facilitating the first step of the catalytic reaction, protonation of the substrate, by the proton donor glutamate. If correct, this will be a novel use for a catalytic triad.

PubMed: 12079387
DOI: 10.1016/S0022-2836(02)00387-X

実験手法

X-RAY DIFFRACTION (1.7 Å)