4fa0 - Revision history

OCA at 15:19, 14 March 2024

2024-03-14T15:19:39Z

← Older revision		Revision as of 15:19, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>
	</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [https://pdbe.org/4fa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa0 ProSAT]</span></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]] 2.65Å</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [https://pdbe.org/4fa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PLAT3_HUMAN PLAT3_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]<ref>PMID:19047760</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:22923616</ref> <ref>PMID:26503625</ref> (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).<ref>PMID:28077878</ref>		[https://www.uniprot.org/uniprot/PLAT3_HUMAN PLAT3_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]<ref>PMID:19047760</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:22923616</ref> <ref>PMID:26503625</ref> (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).<ref>PMID:28077878</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Adipose phospholipase A(2) (AdPLA or Group XVI PLA(2)) plays an important role in the onset of obesity by suppressing adipose tissue lipolysis. As a consequence, AdPLA-deficient mice are resistant to obesity induced by high-fat diet or by leptin deficiency. It has been proposed that AdPLA mediates its anti-lipolytic effects by catalyzing the release of arachidonic acid. Based on sequence homology, AdPLA is part of a small family of acyltransferases and phospholipases related to lecithin:retinol acyltransferases (LRAT). To better understand the enzymatic mechanism of AdPLA and related LRAT proteins, we solved the crystal structure of AdPLA. Our model indicates that AdPLA is structurally related to the NlpC/P60 family of cysteine proteases, having its secondary structure elements configured in a circular permutation of the classic papain fold. Using both structural and biochemical evidence we demonstrate that the enzymatic activity of AdPLA is mediated by a distinctive Cys-His-His catalytic triad and that the C-terminal transmembrane domain of AdPLA is required for the interfacial catalysis. Analysis of the enzymatic activity of AdPLA toward synthetic and natural substrates indicates that AdPLA displays PLA(1) in addition to PLA(2) activity. Thus our results provide insight into the enzymatic mechanism and biochemical properties of AdPLA and LRAT-related proteins, and lead us to propose an alternate mechanism for AdPLA in promoting adipose tissue lipolysis that is not contingent on the release of arachidonic acid and which is compatible with its combined PLA(1)/A(2) activity.

	Structure/Function Relationships of Adipose Phospholipase A2 Containing a Cys-His-His Catalytic Triad.,Pang XY, Cao J, Addington L, Lovell S, Battaile KP, Zhang N, Rao JL, Dennis EA, Moise AR J Biol Chem. 2012 Aug 25. PMID:22923616<ref>PMID:22923616</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4fa0" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==

OCA at 04:44, 7 October 2022

2022-10-07T04:44:06Z

← Older revision		Revision as of 04:44, 7 October 2022
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	==Crystal structure of human AdPLA to 2.65 A resolution==		==Crystal structure of human AdPLA to 2.65 A resolution==
	<StructureSection load='4fa0' size='340' side='right' caption='[[4fa0]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4fa0' size='340' side='right'caption='[[4fa0]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [https://pdbe.org/4fa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa0 ProSAT]</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [~~http~~://pdbe.org/4fa0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fa0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~HRSL3_HUMAN HRSL3_HUMAN]~~] Exhibits ~~PLA1~~/2 activity, catalyzing the calcium-independent ~~hydrolysis~~ of ~~acyl groups in various phosphatidylcholines~~ (~~PC) and phosphatidylethanolamine (PE~~). For most substrates, PLA1 activity is much higher than PLA2 activity. ~~Specifically catalyzes~~ the ~~release~~ of fatty ~~acids~~ from ~~phospholipids in adipose tissue~~ (~~By similarity~~). N- and O-~~acylation~~ activity is ~~hardly detectable. Might decrease protein phosphatase 2A~~ (~~PP2A~~) ~~activity~~.<ref>PMID:~~17374643~~</ref> <ref>PMID:19615464</ref>		[https://www.uniprot.org/uniprot/PLAT3_HUMAN PLAT3_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]<ref>PMID:19047760</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:22923616</ref> <ref>PMID:26503625</ref> (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).<ref>PMID:28077878</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4fa0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fa0" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Phospholipase A2 3D structures\|Phospholipase A2 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Addington, L]]		[[Category: Large Structures]]
	[[Category: Battaile~~, K P~~]]		[[Category: Addington L]]
	[[Category: Lovell, S]]		[[Category: Battaile KP]]
	[[Category: Moise~~, A R~~]]		[[Category: Lovell S]]
	[[Category: Rao~~, J L.U M~~]]		[[Category: Moise AR]]
	[[Category: Zhang, N]]		[[Category: Rao JLUM]]
	~~[[Category: Hrasls3]]~~		[[Category: Zhang N]]
	~~[[Category: Hydrolase]]~~
	~~[[Category: Nlpc/p60 domain]]~~
	~~[[Category: Phospholipase a2]]~~
	~~[[Category: Pla2g16~~]]

OCA at 08:15, 15 November 2017

2017-11-15T08:15:12Z

← Older revision		Revision as of 08:15, 15 November 2017
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	</div>		</div>
	<div class="pdbe-citations 4fa0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fa0" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Phospholipase A2\|Phospholipase A2]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:48, 5 August 2016

2016-08-05T13:48:52Z

← Older revision		Revision as of 13:48, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of human AdPLA to 2.65 A resolution==		==Crystal structure of human AdPLA to 2.65 A resolution==
	<StructureSection load='4fa0' size='340' side='right' caption='[[4fa0]], [[Resolution\|resolution]] 2.65Å' scene=''>		<StructureSection load='4fa0' size='340' side='right' caption='[[4fa0]], [[Resolution\|resolution]] 2.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://pdbe.org/4fa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~PAG16_HUMAN PAG16_HUMAN~~]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:~~19615464~~</ref> <ref>PMID:~~17374643~~</ref>		[[http://www.uniprot.org/uniprot/HRSL3_HUMAN HRSL3_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:17374643</ref> <ref>PMID:19615464</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 17:
	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 4fa0" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Addington, L]]		[[Category: Addington, L]]
	[[Category: Battaile, K P]]		[[Category: Battaile, K P]]

OCA at 03:00, 25 December 2014

2014-12-25T03:00:20Z

← Older revision		Revision as of 03:00, 25 December 2014
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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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/PAG16_HUMAN PAG16_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:19615464</ref> <ref>PMID:17374643</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:45, 9 December 2014

2014-12-09T15:45:21Z

← Older revision		Revision as of 15:45, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:4fa0.~~png\|left\|200px~~]]		==Crystal structure of human AdPLA to 2.65 A resolution==
			<StructureSection load='4fa0' size='340' side='right' caption='[[4fa0]], [[Resolution\|resolution]] 2.65Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4fa0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA0 FirstGlance]. <br>
			</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa0 PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Adipose phospholipase A(2) (AdPLA or Group XVI PLA(2)) plays an important role in the onset of obesity by suppressing adipose tissue lipolysis. As a consequence, AdPLA-deficient mice are resistant to obesity induced by high-fat diet or by leptin deficiency. It has been proposed that AdPLA mediates its anti-lipolytic effects by catalyzing the release of arachidonic acid. Based on sequence homology, AdPLA is part of a small family of acyltransferases and phospholipases related to lecithin:retinol acyltransferases (LRAT). To better understand the enzymatic mechanism of AdPLA and related LRAT proteins, we solved the crystal structure of AdPLA. Our model indicates that AdPLA is structurally related to the NlpC/P60 family of cysteine proteases, having its secondary structure elements configured in a circular permutation of the classic papain fold. Using both structural and biochemical evidence we demonstrate that the enzymatic activity of AdPLA is mediated by a distinctive Cys-His-His catalytic triad and that the C-terminal transmembrane domain of AdPLA is required for the interfacial catalysis. Analysis of the enzymatic activity of AdPLA toward synthetic and natural substrates indicates that AdPLA displays PLA(1) in addition to PLA(2) activity. Thus our results provide insight into the enzymatic mechanism and biochemical properties of AdPLA and LRAT-related proteins, and lead us to propose an alternate mechanism for AdPLA in promoting adipose tissue lipolysis that is not contingent on the release of arachidonic acid and which is compatible with its combined PLA(1)/A(2) activity.

	~~{{STRUCTURE_4fa0\| PDB=4fa0 \| SCENE= }}~~		Structure/Function Relationships of Adipose Phospholipase A2 Containing a Cys-His-His Catalytic Triad.,Pang XY, Cao J, Addington L, Lovell S, Battaile KP, Zhang N, Rao JL, Dennis EA, Moise AR J Biol Chem. 2012 Aug 25. PMID:22923616<ref>PMID:22923616</ref>

	~~===Crystal structure~~ of ~~human AdPLA to 2~~.~~65 A resolution===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22923616}}~~		==See Also==
			*[[Phospholipase A2\|Phospholipase A2]]
	==~~About this Structure~~==		== References ==
	[[~~4fa0~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA0 OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Addington, L.]]		[[Category: Addington, L]]
	[[Category: Battaile, K P.]]		[[Category: Battaile, K P]]
	[[Category: Lovell, S.]]		[[Category: Lovell, S]]
	[[Category: Moise, A R.]]		[[Category: Moise, A R]]
	[[Category: Rao, J L.U M.]]		[[Category: Rao, J L.U M]]
	[[Category: Zhang, N.]]		[[Category: Zhang, N]]
	[[Category: Hrasls3]]		[[Category: Hrasls3]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 10:39, 14 November 2012

2012-11-14T10:39:13Z

← Older revision		Revision as of 10:39, 14 November 2012
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	===Crystal structure of human AdPLA to 2.65 A resolution===		===Crystal structure of human AdPLA to 2.65 A resolution===

			{{ABSTRACT_PUBMED_22923616}}

	==About this Structure==		==About this Structure==

OCA at 07:11, 14 November 2012

2012-11-14T07:11:40Z

← Older revision		Revision as of 07:11, 14 November 2012
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	===Crystal structure of human AdPLA to 2.65 A resolution===		===Crystal structure of human AdPLA to 2.65 A resolution===

	~~{{ABSTRACT_PUBMED_22923616}}~~

	==About this Structure==		==About this Structure==

OCA at 05:23, 5 September 2012

2012-09-05T05:23:37Z

← Older revision		Revision as of 05:23, 5 September 2012
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	[[Image:4fa0.~~jpg~~\|left\|200px]]		[[Image:4fa0.png\|left\|200px]]

	~~<!--~~
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	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
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	{{STRUCTURE_4fa0\| PDB=4fa0 \| SCENE= }}		{{STRUCTURE_4fa0\| PDB=4fa0 \| SCENE= }}

	===Crystal structure of human AdPLA to 2.65 A resolution===		===Crystal structure of human AdPLA to 2.65 A resolution===

			{{ABSTRACT_PUBMED_22923616}}

	==About this Structure==		==About this Structure==

OCA at 07:58, 6 June 2012

2012-06-06T07:58:06Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4fa0.jpg|left|200px]]
-The entry 4fa0 is ON HOLD
+<!--
-Authors: Lovell, Scott, Battaile, Kevin P., Addington, Linsee , Zhang, Na , Rao, J.L. Uma Maheswar, Moise, Alexander R.
+===Crystal structure of human AdPLA to 2.65 A resolution===
-Description: Crystal structure of human AdPLA to 2.65 A resolution