1hvb
From Proteopedia
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CRYSTAL STRUCTURE OF STREPTOMYCES R61 DD-PEPTIDASE COMPLEXED WITH A NOVEL CEPHALOSPORIN ANALOG OF CELL WALL PEPTIDOGLYCAN
Overview
The cell wall imparts structural strength and shape to bacteria. It is, made up of polymeric glycan chains with peptide branches that are, cross-linked to form the cell wall. The cross-linking reaction, catalyzed, by transpeptidases, is the last step in cell wall biosynthesis. These, enzymes are members of the family of penicillin-binding proteins, the, targets of beta-lactam antibiotics. We report herein the structure of a, penicillin-binding protein complexed with a cephalosporin designed to, probe the mechanism of the cross-linking reaction catalyzed by, transpeptidases. The 1.2-A resolution x-ray structure of this, cephalosporin bound to the active site of the bifunctional serine type, D-alanyl-D-alanine carboxypeptidase/transpeptidase (EC ) from Streptomyces, sp. strain R61 reveals how the two peptide strands from the polymeric, substrates are sequestered in the active site of a transpeptidase. The, structure of this complex provides a snapshot of the enzyme and the bound, cell wall components poised for the final and critical cross-linking step, of cell wall biosynthesis.
About this Structure
1HVB is a Single protein structure of sequence from Streptomyces sp. with CEH as ligand. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Full crystallographic information is available from OCA.
Reference
A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis., Lee W, McDonough MA, Kotra L, Li ZH, Silvaggi NR, Takeda Y, Kelly JA, Mobashery S, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1427-31. PMID:11171967
Page seeded by OCA on Tue Nov 20 16:51:16 2007
