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5wze

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'''Unreleased structure'''
 
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The entry 5wze is ON HOLD until Jan 17 2019
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==The structure of Pseudomonas aeruginosa aminopeptidase PepP==
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<StructureSection load='5wze' size='340' side='right' caption='[[5wze]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wze]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WZE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5wze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wze OCA], [http://pdbe.org/5wze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wze RCSB], [http://www.ebi.ac.uk/pdbsum/5wze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wze ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PepP is a virulence-associated gene in Pseudomonas aeruginosa, making it an attractive target for anti-P. aeruginosa drug development. The encoded protein, aminopeptidases P (Pa-PepP), is a type of X-prolyl peptidase that possesses diverse biological functions. The crystal structure verified its canonical pita-bread fold and functional tetrameric assembly, and the functional studies measured the influences of different metal ions on the activity. A trimetal manganese cluster was observed at the active site, elucidating the mechanism of inhibition by metal ions. Additionally, a loop extending from the active site appeared to be important for specific large-substrate binding. Based on the structural comparison and bacterial invasion assays, we showed that this non-conserved surface loop was critical for P. aeruginosa virulence. Taken together, these findings can extend our understanding of the catalytic mechanism and virulence-related functions of Pa-PepP and provide a solid foundation for the design of specific inhibitors against pathogenic-bacterial infections.
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Authors:
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Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.,Peng CT, Liu L, Li CC, He LH, Li T, Shen YL, Gao C, Wang NY, Xia Y, Zhu YB, Song YJ, Lei Q, Yu LT, Bao R Front Microbiol. 2017 Dec 5;8:2385. doi: 10.3389/fmicb.2017.02385. eCollection, 2017. PMID:29259588<ref>PMID:29259588</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5wze" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bao, R]]
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[[Category: He, L H]]
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[[Category: Li, C C]]
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[[Category: Li, T]]
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[[Category: Liu, L]]
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[[Category: Peng, C T]]
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[[Category: Shen, Y L]]
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[[Category: Song, Y J]]
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[[Category: Zhu, Y B]]
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[[Category: Aminopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Pathogenicity]]
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[[Category: Pseudomonas aeruginosa]]

Revision as of 06:57, 17 January 2018

The structure of Pseudomonas aeruginosa aminopeptidase PepP

5wze, resolution 1.78Å

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