1MPX

ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE

Summary for 1MPX

• Entry DOI: 10.2210/pdb1mpx/pdb
• Descriptor: alpha-amino acid ester hydrolase, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: alpha/beta hydrolase, jellyroll, selenomethionine, hydrolase
• Biological source: Xanthomonas citri
• Total number of polymer chains: 4
• Total formula weight: 279603.03

Authors

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. (deposition date: 2002-09-13, release date: 2003-04-15, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)