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1ei5

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{{STRUCTURE_1ei5| PDB=1ei5 | SCENE= }}
{{STRUCTURE_1ei5| PDB=1ei5 | SCENE= }}
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'''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI'''
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===CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI===
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==Overview==
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BACKGROUND: 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. RESULTS: The crystal structure of DAP has been determined to 1.9 A resolution using the multiple isomorphous replacement (MIR) method. The enzyme folds into three domains, A, B and C. Domain A, which contains conserved catalytic residues, has the classical fold of serine beta-lactamases, whereas domains B and C are both antiparallel eight-stranded beta barrels. A loop of domain C protrudes into the substrate-binding site of the enzyme. CONCLUSIONS: Comparison of the biochemical properties and the structure of DAP with PBPs and serine beta-lactamases shows that although the catalytic site of the enzyme is very similar to that of beta-lactamases, its substrate and inhibitor specificity rests on residues of domain C. DAP is a new member of the family of penicillin-recognizing proteins (PRPs) and, at the present time, its enzymatic specificity is clearly unique.
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(as it appears on PubMed at http://www.pubmed.gov), where 10986464 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10986464}}
==About this Structure==
==About this Structure==
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[[Category: D-aminopeptidase]]
[[Category: D-aminopeptidase]]
[[Category: Penicillin binding protein]]
[[Category: Penicillin binding protein]]
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Revision as of 21:44, 30 June 2008

Image:1ei5.png

Template:STRUCTURE 1ei5

CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI

Template:ABSTRACT PUBMED 10986464

About this Structure

1EI5 is a Single protein structure of sequence from Ochrobactrum anthropi. Full crystallographic information is available from OCA.

Reference

Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family., Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J, Structure. 2000 Sep 15;8(9):971-80. PMID:10986464

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