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4k2g
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4k2g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K2G FirstGlance]. <br> | <table><tr><td colspan='2'>[[4k2g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K2G FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1OQ:(2S)-(4-FLUOROPHENYL)[6-(TRIFLUOROMETHYL)PYRIDIN-2-YL]ETHANENITRILE'>1OQ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1OQ:(2S)-(4-FLUOROPHENYL)[6-(TRIFLUOROMETHYL)PYRIDIN-2-YL]ETHANENITRILE'>1OQ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sra|3sra]], [[3srb|3srb]], [[3src|3src]], [[4k2f|4k2f]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sra|3sra]], [[3srb|3srb]], [[3src|3src]], [[4k2f|4k2f]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-homoserine-lactone_acylase Acyl-homoserine-lactone acylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.97 3.5.1.97] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-homoserine-lactone_acylase Acyl-homoserine-lactone acylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.97 3.5.1.97] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k2g RCSB], [http://www.ebi.ac.uk/pdbsum/4k2g PDBsum]</span></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=4k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k2g RCSB], [http://www.ebi.ac.uk/pdbsum/4k2g PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PVDQ_PSEAE PVDQ_PSEAE]] Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of 11 to 14 carbons in length). Degrades 3-oxo-C12-HSL, one of the two main AHL signal molecules of P.aeruginosa, and thereby functions as a quorum quencher, inhibiting the las quorum-sensing system. Therefore, may enable P.aeruginosa to modulate its own quorum-sensing-dependent pathogenic potential. Also appears to be required for pyoverdin biosynthesis.<ref>PMID:16495538</ref> <ref>PMID:14532048</ref> <ref>PMID:12686626</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acyl-homoserine-lactone acylase]] | [[Category: Acyl-homoserine-lactone acylase]] | ||
| - | [[Category: Drake, E J | + | [[Category: Drake, E J]] |
| - | [[Category: Gulick, A M | + | [[Category: Gulick, A M]] |
| - | [[Category: Munoz, B | + | [[Category: Munoz, B]] |
| - | [[Category: Theriault, J R | + | [[Category: Theriault, J R]] |
| - | [[Category: Wurst, J M | + | [[Category: Wurst, J M]] |
[[Category: Amidohydrolase]] | [[Category: Amidohydrolase]] | ||
[[Category: Bacterial protein]] | [[Category: Bacterial protein]] | ||
Revision as of 16:50, 25 December 2014
Structure of Pseudomonas aeruginosa PvdQ bound to BRD-A33442372
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Categories: Acyl-homoserine-lactone acylase | Drake, E J | Gulick, A M | Munoz, B | Theriault, J R | Wurst, J M | Amidohydrolase | Bacterial protein | Catalytic domain | High-throughput screening assay | Hydrolase-hydrolase inhibitor complex | Molecular sequence data | Oligopeptide | Small molecule library | Structure-activity relationship
