1MPX

ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE

1MPX の概要

• エントリーDOI: 10.2210/pdb1mpx/pdb
• 分子名称: alpha-amino acid ester hydrolase, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase, jellyroll, selenomethionine, hydrolase
• 由来する生物種: Xanthomonas citri
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 279603.03

構造登録者

Barends, T.R.M.,Polderman-Tijmes, J.J.,Jekel, P.A.,Hensgens, C.M.H.,de Vries, E.J.,Janssen, D.B.,Dijkstra, B.W. (登録日: 2002-09-13, 公開日: 2003-04-15, 最終更新日: 2024-10-30)

主引用文献

Barends, T.R.,Polderman-Tijmes, J.J.,Jekel, P.A.,Hensgens, C.M.,de Vries, E.J.,Janssen, D.B.,Dijkstra, B.W.
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases.
J.Biol.Chem., 278:23076-23084, 2003

PubMed Abstract: alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and synthesis of esters and amides with an alpha-amino group. As such, they can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam nuclei obtained from the hydrolysis of natural antibiotics. This article describes the gene sequence and the 1.9-A resolution crystal structure of the AEH from Xanthomonas citri. The enzyme consists of an alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll beta-domain. Structural homology was observed to the Rhodococcus cocaine esterase, indicating that both enzymes belong to the same class of bacterial hydrolases. Docking of a beta-lactam antibiotic in the active site explains the substrate specificity, specifically the necessity of an alpha-amino group on the substrate, and explains the low specificity toward the beta-lactam nucleus.

PubMed: 12684501
DOI: 10.1074/jbc.M302246200

実験手法

X-RAY DIFFRACTION (1.9 Å)