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| - | [[Image:1ei5.jpg|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI== |
| - | |PDB= 1ei5 |SIZE=350|CAPTION= <scene name='initialview01'>1ei5</scene>, resolution 1.9Å
| + | <StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution|resolution]] 1.90Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_anthropi Brucella anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI5 FirstGlance]. <br> |
| - | |ACTIVITY= <span class='plainlinks'>[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] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [https://pdbe.org/1ei5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY= | + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB]</span> | + | [https://www.uniprot.org/uniprot/DAP_BRUAN DAP_BRUAN] Hydrolyzes N-terminal residues in D-amino acid-containing peptides. |
| - | }}
| + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/1ei5_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ei5 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI'''
| + | ==See Also== |
| - | | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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.
| + | [[Category: Brucella anthropi]] |
| - | | + | [[Category: Large Structures]] |
| - | ==About this Structure==
| + | [[Category: Bompard-Gilles C]] |
| - | 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].
| + | [[Category: Fanuel L]] |
| - | | + | [[Category: Frere J-M]] |
| - | ==Reference==
| + | [[Category: Joris J]] |
| - | 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: Prange T]] |
| - | [[Category: D-stereospecific aminopeptidase]] | + | [[Category: Remaut H]] |
| - | [[Category: Ochrobactrum anthropi]]
| + | [[Category: Van Beeumen J]] |
| - | [[Category: Single protein]] | + | [[Category: Villeret V]] |
| - | [[Category: Beeumen, J Van.]]
| + | |
| - | [[Category: Bompard-Gilles, C.]] | + | |
| - | [[Category: Fanuel, L.]] | + | |
| - | [[Category: Frere, J M.]] | + | |
| - | [[Category: Joris, J.]] | + | |
| - | [[Category: Prange, T.]] | + | |
| - | [[Category: Remaut, H.]] | + | |
| - | [[Category: Villeret, V.]] | + | |
| - | [[Category: alpha/beta domain]] | + | |
| - | [[Category: beta barrel domain]]
| + | |
| - | [[Category: d-aminopeptidase]]
| + | |
| - | [[Category: penicillin binding protein]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:03:13 2008''
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