|
|
| (One intermediate revision by the same user not shown) |
| Line 3: |
Line 3: |
| <StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br> | | <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> |
| </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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> | | </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> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ei5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 ProSAT]</span></td></tr> | | <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> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/DAP_OCHAN DAP_OCHAN]] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.[HAMAP-Rule:MF_01960] | | [https://www.uniprot.org/uniprot/DAP_BRUAN DAP_BRUAN] Hydrolyzes N-terminal residues in D-amino acid-containing peptides. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 19: |
Line 19: |
| </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]. | | </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> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| 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.
| |
|
| |
| 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<ref>PMID:10986464</ref>
| |
|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 49188]] | | [[Category: Brucella anthropi]] |
| [[Category: D-stereospecific aminopeptidase]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Beeumen, J Van]]
| | [[Category: Bompard-Gilles C]] |
| [[Category: Bompard-Gilles, C]] | | [[Category: Fanuel L]] |
| [[Category: Fanuel, L]] | | [[Category: Frere J-M]] |
| [[Category: Frere, J M]] | | [[Category: Joris J]] |
| [[Category: Joris, J]] | | [[Category: Prange T]] |
| [[Category: Prange, T]] | | [[Category: Remaut H]] |
| [[Category: Remaut, H]] | | [[Category: Van Beeumen J]] |
| [[Category: Villeret, V]] | | [[Category: Villeret V]] |
| [[Category: Alpha/beta domain]] | |
| [[Category: Beta barrel domain]]
| |
| [[Category: D-aminopeptidase]]
| |
| [[Category: Hydrolase]]
| |
| [[Category: Penicillin binding protein]]
| |