1ei5
From Proteopedia
(New page: 200px<br /><applet load="1ei5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ei5, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ei5.jpg|left|200px]]<br /><applet load="1ei5" size=" | + | [[Image:1ei5.jpg|left|200px]]<br /><applet load="1ei5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ei5, resolution 1.9Å" /> | caption="1ei5, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI'''<br /> | '''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: beta-Lactam compounds are the most widely used antibiotics. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Active as [http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] Full crystallographic information is available from [http:// | + | 1EI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Active as [http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ochrobactrum anthropi]] | [[Category: Ochrobactrum anthropi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beeumen, J | + | [[Category: Beeumen, J Van.]] |
[[Category: Bompard-Gilles, C.]] | [[Category: Bompard-Gilles, C.]] | ||
[[Category: Fanuel, L.]] | [[Category: Fanuel, L.]] | ||
| - | [[Category: Frere, J | + | [[Category: Frere, J M.]] |
[[Category: Joris, J.]] | [[Category: Joris, J.]] | ||
[[Category: Prange, T.]] | [[Category: Prange, T.]] | ||
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[[Category: penicillin binding protein]] | [[Category: penicillin binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:01 2008'' |
Revision as of 10:28, 21 February 2008
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CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI
Overview
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.
About this Structure
1EI5 is a Single protein structure of sequence from Ochrobactrum anthropi. Active as D-stereospecific aminopeptidase, with EC number 3.4.11.19 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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