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1hd8
From Proteopedia
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Revision as of 13:29, 30 October 2007
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CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 AT 2.3 A RESOLUTION
Overview
Penicillin-binding protein 5 (PBP 5) of Escherichia coli functions as a, d-alanine carboxypeptidase, cleaving the C-terminal d-alanine residue from, cell wall peptides. Like all PBPs, PBP 5 forms a covalent acyl-enzyme, complex with beta-lactam antibiotics; however, PBP 5 is distinguished by, its high rate of deacylation of the acyl-enzyme complex (t(12), approximately 9 min). A Gly-105 --> Asp mutation in PBP 5 markedly impairs, this beta-lactamase activity (deacylation), with only minor effects on, acylation, and promotes accumulation of a covalent complex with peptide, substrates. To gain further insight into the catalytic mechanism of PBP 5, we determined the three-dimensional structure of the G105D mutant form of, soluble PBP 5 (termed sPBP 5') at 2.3 A resolution. The structure ... [(full description)]
About this Structure
1HD8 is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [3.4.16.4]. Structure known Active Site: S44. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution., Davies C, White SW, Nicholas RA, J Biol Chem. 2001 Jan 5;276(1):616-23. PMID:10967102
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