5wze: Difference between revisions
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The | ==The structure of Pseudomonas aeruginosa aminopeptidase PepP== | ||
<StructureSection load='5wze' size='340' side='right' caption='[[5wze]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5wze" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bao, R]] | |||
[[Category: He, L H]] | |||
[[Category: Li, C C]] | |||
[[Category: Li, T]] | |||
[[Category: Liu, L]] | |||
[[Category: Peng, C T]] | |||
[[Category: Shen, Y L]] | |||
[[Category: Song, Y J]] | |||
[[Category: Zhu, Y B]] | |||
[[Category: Aminopeptidase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Pathogenicity]] | |||
[[Category: Pseudomonas aeruginosa]] | |||
