3l94 - Revision history

OCA at 08:45, 7 February 2024

OCA — Wed, 07 Feb 2024 08:45:50 GMT

←Older revision		Revision as of 08:45, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='3l94' size='340' side='right'caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3l94' size='340' side='right'caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L94 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L94 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1,2~~-~~ETHANEDIOL'>EDO</scene>~~, ~~<scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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]] 1.95Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3l91\|3l91]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PA2385, pvdQ, qsc112 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~287~~ "~~Bacillus aeruginosus~~" ~~(Schroeter 1872) Trevisan 1885])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Acyl-homoserine-lactone_acylase Acyl-homoserine-lactone acylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.97 3.5.1.97]~~ </~~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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [https://pdbe.org/3l94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [https://www.ebi.ac.uk/pdbsum/3l94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l94 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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [https://pdbe.org/3l94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [https://www.ebi.ac.uk/pdbsum/3l94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l94 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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>	+	[https://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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The human pathogen Pseudomonas aeruginosa produces a variety of virulence factors including pyoverdine, a nonribosomally produced peptide siderophore. The maturation pathway of the pyoverdine peptide is complex and provides a unique target for inhibition. Within the pyoverdine biosynthetic cluster is a periplasmic hydrolase, PvdQ, that is required for pyoverdine production. However, the precise role of PvdQ in the maturation pathway has not been biochemically characterized. We demonstrate herein that the initial module of the nonribosomal peptide synthetase PvdL adds a myristate moiety to the pyoverdine precursor. We extracted this acylated precursor, called PVDIq, from a pvdQ mutant strain and show that the PvdQ enzyme removes the fatty acid catalyzing one of the final steps in pyoverdine maturation. Incubation of PVDIq with crystals of PvdQ allowed us to capture the acylated enzyme and confirm through structural studies the chemical composition of the incorporated acyl chain. Finally, because inhibition of siderophore synthesis has been identified as a potential antibiotic strategy, we developed a high-throughput screening assay and tested a small chemical library for compounds that inhibit PvdQ activity. Two compounds that block PvdQ have been identified, and their binding within the fatty acid binding pocket was structurally characterized.	+
-		+
-	Structural Characterization and High-Throughput Screening of Inhibitors of PvdQ, an NTN Hydrolase Involved in Pyoverdine Synthesis.,Drake EJ, Gulick AM ACS Chem Biol. 2011 Sep 15. PMID:21892836<ref>PMID:21892836</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3l94" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Acyl-homoserine-lactone acylase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Drake, E J~~]]	+	[[Category: Pseudomonas aeruginosa]]
-	[[Category: ~~Gulick, A M~~]]	+	[[Category: Drake EJ]]
-	[[Category: ~~Acylase]]~~	+	[[Category: Gulick AM]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ntn hydrolase]]~~	+
-	~~[[Category: Pvdq]]~~	+
-	~~[[Category: Pyoverdine]]~~	+
-	~~[[Category: Quorum sensing]]~~	+
-	~~[[Category: Zymogen~~]]	+

OCA at 13:38, 4 May 2022

OCA — Wed, 04 May 2022 13:38:15 GMT

←Older revision		Revision as of 13:38, 4 May 2022
Line 1:		Line 1:

	==Structure of PvdQ covalently acylated with myristate==		==Structure of PvdQ covalently acylated with myristate==
-	<StructureSection load='3l94' size='340' side='right' caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='3l94' size='340' side='right'caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3L94 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L94 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3l91\|3l91]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, pvdQ, qsc112 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, pvdQ, qsc112 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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 id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acyl-homoserine-lactone_acylase Acyl-homoserine-lactone acylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.97 3.5.1.97] </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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [~~http~~://pdbe.org/3l94 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3l94 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3l94 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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [https://pdbe.org/3l94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [https://www.ebi.ac.uk/pdbsum/3l94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l94 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>	+	[[https://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 ==
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Acyl-homoserine-lactone acylase]]		[[Category: Acyl-homoserine-lactone acylase]]
		+	[[Category: Large Structures]]
	[[Category: Drake, E J]]		[[Category: Drake, E J]]
	[[Category: Gulick, A M]]		[[Category: Gulick, A M]]

OCA at 16:32, 4 August 2016

OCA — Thu, 04 Aug 2016 16:32:54 GMT

←Older revision		Revision as of 16:32, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of PvdQ covalently acylated with myristate==		==Structure of PvdQ covalently acylated with myristate==
	<StructureSection load='3l94' size='340' side='right' caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3l94' size='340' side='right' caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pseudomonas_aeruginosa Pseudomonas aeruginosa~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L94 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L94 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, pvdQ, qsc112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 ~~Pseudomonas aeruginosa~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, pvdQ, qsc112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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 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 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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [http://www.ebi.ac.uk/pdbsum/3l94 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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [http://pdbe.org/3l94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [http://www.ebi.ac.uk/pdbsum/3l94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l94 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3l94" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Acyl-homoserine-lactone acylase]]		[[Category: Acyl-homoserine-lactone acylase]]
-	[[Category: Pseudomonas aeruginosa]]
	[[Category: Drake, E J]]		[[Category: Drake, E J]]
	[[Category: Gulick, A M]]		[[Category: Gulick, A M]]

OCA at 11:01, 25 December 2014

OCA — Thu, 25 Dec 2014 11:01:30 GMT

←Older revision		Revision as of 11:01, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}~~	+	==Structure of PvdQ covalently acylated with myristate==
-	===Structure of PvdQ covalently acylated with myristate===	+	<StructureSection load='3l94' size='340' side='right' caption='[[3l94]], [[Resolution\|resolution]] 1.95Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21892836}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L94 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, pvdQ, qsc112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</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 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=3l94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l94 RCSB], [http://www.ebi.ac.uk/pdbsum/3l94 PDBsum]</span></td></tr>
		+	</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>		[[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;">
		+	== Publication Abstract from PubMed ==
		+	The human pathogen Pseudomonas aeruginosa produces a variety of virulence factors including pyoverdine, a nonribosomally produced peptide siderophore. The maturation pathway of the pyoverdine peptide is complex and provides a unique target for inhibition. Within the pyoverdine biosynthetic cluster is a periplasmic hydrolase, PvdQ, that is required for pyoverdine production. However, the precise role of PvdQ in the maturation pathway has not been biochemically characterized. We demonstrate herein that the initial module of the nonribosomal peptide synthetase PvdL adds a myristate moiety to the pyoverdine precursor. We extracted this acylated precursor, called PVDIq, from a pvdQ mutant strain and show that the PvdQ enzyme removes the fatty acid catalyzing one of the final steps in pyoverdine maturation. Incubation of PVDIq with crystals of PvdQ allowed us to capture the acylated enzyme and confirm through structural studies the chemical composition of the incorporated acyl chain. Finally, because inhibition of siderophore synthesis has been identified as a potential antibiotic strategy, we developed a high-throughput screening assay and tested a small chemical library for compounds that inhibit PvdQ activity. Two compounds that block PvdQ have been identified, and their binding within the fatty acid binding pocket was structurally characterized.

-	~~==About this Structure==~~	+	Structural Characterization and High-Throughput Screening of Inhibitors of PvdQ, an NTN Hydrolase Involved in Pyoverdine Synthesis.,Drake EJ, Gulick AM ACS Chem Biol. 2011 Sep 15. PMID:21892836<ref>PMID:21892836</ref>
-	~~[[3l94]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:021892836</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Acyl-homoserine-lactone acylase]]		[[Category: Acyl-homoserine-lactone acylase]]
	[[Category: Pseudomonas aeruginosa]]		[[Category: Pseudomonas aeruginosa]]
-	[[Category: Drake, E J.]]	+	[[Category: Drake, E J]]
-	[[Category: Gulick, A M.]]	+	[[Category: Gulick, A M]]
	[[Category: Acylase]]		[[Category: Acylase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 19:13, 17 April 2013

OCA — Wed, 17 Apr 2013 19:13:32 GMT

←Older revision		Revision as of 19:13, 17 April 2013
Line 1:		Line 1:
	{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}		{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}
	===Structure of PvdQ covalently acylated with myristate===		===Structure of PvdQ covalently acylated with myristate===
		+	{{ABSTRACT_PUBMED_21892836}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:021892836</ref><references group="xtra"/><references/>
	[[Category: Acyl-homoserine-lactone acylase]]		[[Category: Acyl-homoserine-lactone acylase]]
	[[Category: Pseudomonas aeruginosa]]		[[Category: Pseudomonas aeruginosa]]

OCA at 20:22, 4 April 2013

OCA — Thu, 04 Apr 2013 20:22:38 GMT

←Older revision		Revision as of 20:22, 4 April 2013
Line 1:		Line 1:
-	[[Image:3l94.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3l94", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}		{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}
-
	===Structure of PvdQ covalently acylated with myristate===		===Structure of PvdQ covalently acylated with myristate===

		+	==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>

	==About this Structure==		==About this Structure==
	[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA].		[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Acyl-homoserine-lactone acylase]]		[[Category: Acyl-homoserine-lactone acylase]]
	[[Category: Pseudomonas aeruginosa]]		[[Category: Pseudomonas aeruginosa]]
	[[Category: Drake, E J.]]		[[Category: Drake, E J.]]
	[[Category: Gulick, A M.]]		[[Category: Gulick, A M.]]
		+	[[Category: Acylase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ntn hydrolase]]
		+	[[Category: Pvdq]]
		+	[[Category: Pyoverdine]]
		+	[[Category: Quorum sensing]]
		+	[[Category: Zymogen]]

OCA: Protected "3l94" [edit=sysop:move=sysop]

OCA — Wed, 26 Jan 2011 13:02:18 GMT

Protected "3l94" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:02, 26 January 2011

OCA at 13:02, 26 January 2011

OCA — Wed, 26 Jan 2011 13:02:15 GMT

←Older revision		Revision as of 13:02, 26 January 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3l94.jpg\|left\|200px]]

-	The ~~entry 3l94~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3l94", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3l94\| PDB=3l94 \| SCENE= }}

-	~~Authors: Drake, E.J., Gulick, A.M.~~	+	===Structure of PvdQ covalently acylated with myristate===

-	Description: Structure of PvdQ covalently acylated with myristate

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Dec 22 09~~:31:~~22 2010''~~	+	==About this Structure==
		+	[[3l94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L94 OCA].
		+	[[Category: Acyl-homoserine-lactone acylase]]
		+	[[Category: Pseudomonas aeruginosa]]
		+	[[Category: Drake, E J.]]
		+	[[Category: Gulick, A M.]]

OCA at 06:18, 22 December 2010

OCA — Wed, 22 Dec 2010 06:18:45 GMT

←Older revision		Revision as of 06:18, 22 December 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3l94 is ON HOLD	+	The entry 3l94 is ON HOLD until Paper Publication

	Authors: Drake, E.J., Gulick, A.M.		Authors: Drake, E.J., Gulick, A.M.
Line 7:		Line 7:
	Description: Structure of PvdQ covalently acylated with myristate		Description: Structure of PvdQ covalently acylated with myristate

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jan 13 13~~:37:28 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:31:22 2010''

OCA: New page: '''Unreleased structure''' The entry 3l94 is ON HOLD Authors: Drake, E.J., Gulick, A.M. Description: Structure of PvdQ covalently acylated with myristate ''Page seeded by [http://oca....

OCA — Wed, 13 Jan 2010 11:37:29 GMT

New page: '''Unreleased structure''' The entry 3l94 is ON HOLD Authors: Drake, E.J., Gulick, A.M. Description: Structure of PvdQ covalently acylated with myristate ''Page seeded by [http://oca....

New page

'''Unreleased structure'''

The entry 3l94 is ON HOLD

Authors: Drake, E.J., Gulick, A.M.

Description: Structure of PvdQ covalently acylated with myristate

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 13 13:37:28 2010''