This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ei5
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ei5.jpg|left|200px]] | + | [[Image:1ei5.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI''' | + | {{Structure |
| + | |PDB= 1ei5 |SIZE=350|CAPTION= <scene name='initialview01'>1ei5</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1EI5 is a [ | + | 1EI5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10986464 10986464] |
[[Category: D-stereospecific aminopeptidase]] | [[Category: D-stereospecific aminopeptidase]] | ||
[[Category: Ochrobactrum anthropi]] | [[Category: Ochrobactrum anthropi]] | ||
| Line 27: | Line 36: | ||
[[Category: penicillin binding protein]] | [[Category: penicillin binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:54 2008'' |
Revision as of 08:55, 20 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | D-stereospecific aminopeptidase, with EC number 3.4.11.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 10:55:54 2008
