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pubmed-article:11171967pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:11171967pubmed:pagination1427-31lld:pubmed
pubmed-article:11171967pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:11171967pubmed:articleTitleA 1.2-A snapshot of the final step of bacterial cell wall biosynthesis.lld:pubmed
pubmed-article:11171967pubmed:affiliationDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA.lld:pubmed
pubmed-article:11171967pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11171967pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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