1ei5: Difference between revisions

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<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [https://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]] 1.9&#8491;</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>
<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 ==
[[https://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]]
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</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&reg;/PubMed&reg;, 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]]

Latest revision as of 10:03, 7 February 2024

CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPICRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI

Structural highlights

1ei5 is a 1 chain structure with sequence from Brucella anthropi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAP_BRUAN Hydrolyzes N-terminal residues in D-amino acid-containing peptides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ei5, resolution 1.90Å

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