3src - Revision history

OCA at 09:41, 30 October 2024

2024-10-30T09:41:45Z

← Older revision		Revision as of 09:41, 30 October 2024
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	== 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 3src" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:05, 14 March 2024

2024-03-14T13:05:37Z

← Older revision		Revision as of 13:05, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3src' size='340' side='right'caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3src' size='340' side='right'caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3src]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Pseae Pseae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SRC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3src]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SRC FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=28N:8-BROMO-4H~~-[~~1,2,4]OXADIAZOLO~~[~~3,4-C~~]~~[1,4~~]~~BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,~~2~~-ETHANEDIOL'>EDO</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]] 2Å</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]]~~, ~~[[3l94\|3l94]]~~, ~~[[2wyb\|2wyb~~]], [~~[2wyc\|2wyc]]~~, ~~[[2wyd\|2wyd~~]], [~~[2wye\|2wye]]~~, ~~[[3sra\|3sra~~]~~], [[3srb\|3srb]]</div></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	~~<tr id='gene~~'>~~<td class="sblockLbl"><b>[[Gene\|Gene:]]~~</~~b></td><td class="sblockDat"~~>~~PA2385, PA2385 PvdQ~~, ~~qsc112 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])~~<~~/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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [https://pdbe.org/3src PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [https://www.ebi.ac.uk/pdbsum/3src PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3src 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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [https://pdbe.org/3src PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [https://www.ebi.ac.uk/pdbsum/3src PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3src 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 3src" 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: ~~Pseae~~]]		[[Category: Pseudomonas aeruginosa PAO1]]
	[[Category: Drake~~, E J~~]]		[[Category: Drake EJ]]
	[[Category: Gulick~~, A M]]~~		[[Category: Gulick AM]]
	~~[[Category: Acylase]]~~
	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~
	~~[[Category: Liganded]]~~
	~~[[Category: Nrps tailoring~~]]

OCA at 08:07, 29 June 2022

2022-06-29T08:07:25Z

← Older revision		Revision as of 08:07, 29 June 2022
Line 1:		Line 1:

	==Structure of Pseudomonas aeruginosa PvdQ bound to NS2028==		==Structure of Pseudomonas aeruginosa PvdQ bound to NS2028==
	<StructureSection load='3src' size='340' side='right' caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3src' size='340' side='right'caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3src]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3SRC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3src]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SRC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</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]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, PA2385 PvdQ, qsc112 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, PA2385 PvdQ, qsc112 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [~~http~~://pdbe.org/3src PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3src PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3src 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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [https://pdbe.org/3src PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [https://www.ebi.ac.uk/pdbsum/3src PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3src 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: Pseae]]		[[Category: Pseae]]
	[[Category: Drake, E J]]		[[Category: Drake, E J]]

OCA at 07:17, 4 August 2016

2016-08-04T07:17:39Z

← Older revision		Revision as of 07:17, 4 August 2016
Line 1:		Line 1:

	==Structure of Pseudomonas aeruginosa PvdQ bound to NS2028==		==Structure of Pseudomonas aeruginosa PvdQ bound to NS2028==
	<StructureSection load='3src' size='340' side='right' caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3src' size='340' side='right' caption='[[3src]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3src]] 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=3SRC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SRC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3src]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SRC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, 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, PA2385 PvdQ, qsc112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [http://www.ebi.ac.uk/pdbsum/3src 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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [http://pdbe.org/3src PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [http://www.ebi.ac.uk/pdbsum/3src PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3src 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 3src" 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: Pseae]]
	[[Category: Drake, E J]]		[[Category: Drake, E J]]
	[[Category: Gulick, A M]]		[[Category: Gulick, A M]]

OCA at 06:50, 25 December 2014

2014-12-25T06:50:38Z

← Older revision		Revision as of 06:50, 25 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3src]] 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=3SRC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SRC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3src]] 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=3SRC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SRC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28N:8-BROMO-4H-[1,2,4]OXADIAZOLO[3,4-C][1,4]BENZOXAZIN-1-ONE'>28N</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">[[3l91\|3l91]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l91\|3l91]], [[3l94\|3l94]], [[2wyb\|2wyb]], [[2wyc\|2wyc]], [[2wyd\|2wyd]], [[2wye\|2wye]], [[3sra\|3sra]], [[3srb\|3srb]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PA2385, 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, PA2385 PvdQ, qsc112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [http://www.ebi.ac.uk/pdbsum/3src 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=3src FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3src OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3src RCSB], [http://www.ebi.ac.uk/pdbsum/3src 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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	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>		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 ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
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	[[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-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Liganded]]		[[Category: Liganded]]
	[[Category: Nrps tailoring]]		[[Category: Nrps tailoring]]

OCA at 05:18, 5 June 2014

2014-06-05T05:18:54Z

@@ Line 1: / Line 1: @@
-[[Image:3src.png|left|200px]]
+==Structure of Pseudomonas aeruginosa PvdQ bound to NS2028==
-<!--
+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>
-===Structure of Pseudomonas aeruginosa PvdQ bound to NS2028===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_21892836}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 21892836 is the PubMed ID number.
+</StructureSection>
 [[Category: Acyl-homoserine-lactone acylase]]
 [[Category: Pseudomonas aeruginosa]]

OCA at 05:24, 30 November 2011

2011-11-30T05:24:58Z

← Older revision		Revision as of 05:24, 30 November 2011
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	[[Image:3src.~~jpg~~\|left\|200px]]		[[Image:3src.png\|left\|200px]]

	<!--		<!--

OCA at 05:53, 21 September 2011

2011-09-21T05:53:20Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3src.jpg|left|200px]]
-The entry 3src is ON HOLD  until Paper Publication
+<!--
-Authors: Gulick, A.M., Drake, E.J.
+===Structure of Pseudomonas aeruginosa PvdQ bound to NS2028===
-Description: Structure of Pseudomonas aeruginosa PvdQ bound to NS2028

OCA at 05:41, 27 July 2011

2011-07-27T05:41:23Z

← Older revision		Revision as of 05:41, 27 July 2011
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3src is ON HOLD		The entry 3src is ON HOLD until Paper Publication

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

	Description: Structure of Pseudomonas aeruginosa PvdQ bound to NS2028		Description: Structure of Pseudomonas aeruginosa PvdQ bound to NS2028

OCA at 06:14, 20 July 2011

2011-07-20T06:14:30Z

← Older revision		Revision as of 06:14, 20 July 2011
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	Authors: Gulick, A.M., Drake, E.J.		Authors: Gulick, A.M., Drake, E.J.

	Description: Structure of Pseudomonas aeruginosa bound to NS2028		Description: Structure of Pseudomonas aeruginosa PvdQ bound to NS2028