1EI5

CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI

Summary for 1EI5

• Entry DOI: 10.2210/pdb1ei5/pdb
• Descriptor: D-AMINOPEPTIDASE (2 entities in total)
• Functional Keywords: d-aminopeptidase, penicillin binding protein, alpha/beta domain, beta barrel domain, hydrolase
• Biological source: Ochrobactrum anthropi
• Total number of polymer chains: 1
• Total formula weight: 57458.75

Authors

Bompard-Gilles, C.,Remaut, H.,Villeret, V.,Prange, T.,Fanuel, L.,Joris, J.,Frere, J.-M.,Van Beeumen, J. (deposition date: 2000-02-24, release date: 2000-10-04, Last modification date: 2024-02-07)

Primary citation

Bompard-Gilles, C.,Remaut, H.,Villeret, V.,Prange, T.,Fanuel, L.,Delmarcelle, M.,Joris, B.,Frere, J.,Van Beeumen, J.
Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.
Structure Fold.Des., 8:971-980, 2000

PubMed Abstract: beta-Lactam compounds are the most widely used antibiotics. They inactivate bacterial DD-transpeptidases, also called penicillin-binding proteins (PBPs), involved in cell-wall biosynthesis. The most common bacterial resistance mechanism against beta-lactam compounds is the synthesis of beta-lactamases that hydrolyse beta-lactam rings. These enzymes are believed to have evolved from cell-wall DD-peptidases. Understanding the biochemical and mechanistic features of the beta-lactam targets is crucial because of the increasing number of resistant bacteria. DAP is a D-aminopeptidase produced by Ochrobactrum anthropi. It is inhibited by various beta-lactam compounds and shares approximately 25% sequence identity with the R61 DD-carboxypeptidase and the class C beta-lactamases.

PubMed: 10986464
DOI: 10.1016/S0969-2126(00)00188-X

Experimental method

X-RAY DIFFRACTION (1.9 Å)