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1hd8

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{{STRUCTURE_1hd8| PDB=1hd8 | SCENE= }}
{{STRUCTURE_1hd8| PDB=1hd8 | SCENE= }}
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'''CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 AT 2.3 A RESOLUTION'''
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===CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 AT 2.3 A RESOLUTION===
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==Overview==
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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 --&gt; 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 is composed of two domains, a penicillin binding domain with a striking similarity to Class A beta-lactamases (TEM-1-like) and a domain of unknown function. In addition, the penicillin-binding domain contains an active site loop spatially equivalent to the Omega loop of beta-lactamases. In beta-lactamases, the Omega loop contains two amino acids involved in catalyzing deacylation. This similarity may explain the high beta-lactamase activity of wild-type PBP 5. Because of the low rate of deacylation of the G105D mutant, visualization of peptide substrates bound to the active site may be possible.
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{{ABSTRACT_PUBMED_10967102}}
==About this Structure==
==About this Structure==
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[[Category: Penicillin-binding protein]]
[[Category: Penicillin-binding protein]]
[[Category: Peptidoglycan synthesis]]
[[Category: Peptidoglycan synthesis]]
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Revision as of 05:01, 1 July 2008

Image:1hd8.png

Template:STRUCTURE 1hd8

CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 AT 2.3 A RESOLUTION

Template:ABSTRACT PUBMED 10967102

About this Structure

1HD8 is a Single protein structure of sequence from Escherichia coli. 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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