5w7b - Revision history

OCA at 08:29, 8 January 2020

OCA — Wed, 08 Jan 2020 08:29:01 GMT

←Older revision		Revision as of 08:29, 8 January 2020
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	==Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS==		==Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS==
-	<StructureSection load='5w7b' size='340' side='right' caption='[[5w7b]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5w7b' size='340' side='right'caption='[[5w7b]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5w7b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7B FirstGlance]. <br>		<table><tr><td colspan='2'>[[5w7b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7B FirstGlance]. <br>
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	[[Category: Acyloxyacyl hydrolase]]		[[Category: Acyloxyacyl hydrolase]]
	[[Category: European rabbit]]		[[Category: European rabbit]]
		+	[[Category: Large Structures]]
	[[Category: Gorelik, A]]		[[Category: Gorelik, A]]
	[[Category: Illes, K]]		[[Category: Illes, K]]

OCA at 07:08, 31 January 2018

OCA — Wed, 31 Jan 2018 07:08:02 GMT

←Older revision		Revision as of 07:08, 31 January 2018
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AOAH_RABIT AOAH_RABIT]] Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.[UniProtKB:O35298]		[[http://www.uniprot.org/uniprot/AOAH_RABIT AOAH_RABIT]] Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.[UniProtKB:O35298]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	LPS is a potent bacterial endotoxin that triggers the innate immune system. Proper recognition of LPS by pattern-recognition receptors requires a full complement of typically six acyl chains in the lipid portion. Acyloxyacyl hydrolase (AOAH) is a host enzyme that removes secondary (acyloxyacyl-linked) fatty acids from LPS, rendering it immunologically inert. This activity is critical for recovery from immune tolerance that follows Gram-negative infection. To understand the molecular mechanism of AOAH function, we determined its crystal structure and its complex with LPS. The substrate's lipid moiety is accommodated in a large hydrophobic pocket formed by the saposin and catalytic domains with a secondary acyl chain inserted into a narrow lateral hydrophobic tunnel at the active site. The enzyme establishes dispensable contacts with the phosphate groups of LPS but does not interact with its oligosaccharide portion. Proteolytic processing allows movement of an amphipathic helix possibly involved in substrate access at membranes.
		+
		+	Crystal structure of the mammalian lipopolysaccharide detoxifier.,Gorelik A, Illes K, Nagar B Proc Natl Acad Sci U S A. 2018 Jan 17. pii: 1719834115. doi:, 10.1073/pnas.1719834115. PMID:29343645<ref>PMID:29343645</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5w7b" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:16, 17 January 2018

OCA — Wed, 17 Jan 2018 08:16:40 GMT

←Older revision		Revision as of 08:16, 17 January 2018
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	<StructureSection load='5w7b' size='340' side='right' caption='[[5w7b]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5w7b' size='340' side='right' caption='[[5w7b]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5w7b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5w7b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7B FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PA1:2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE'>PA1</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PA1:2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE'>PA1</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AOAH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyloxyacyl_hydrolase Acyloxyacyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.77 3.1.1.77] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyloxyacyl_hydrolase Acyloxyacyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.77 3.1.1.77] </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=5w7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7b OCA], [http://pdbe.org/5w7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7b RCSB], [http://www.ebi.ac.uk/pdbsum/5w7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7b 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=5w7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7b OCA], [http://pdbe.org/5w7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7b RCSB], [http://www.ebi.ac.uk/pdbsum/5w7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7b ProSAT]</span></td></tr>
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	</StructureSection>		</StructureSection>
	[[Category: Acyloxyacyl hydrolase]]		[[Category: Acyloxyacyl hydrolase]]
		+	[[Category: European rabbit]]
	[[Category: Gorelik, A]]		[[Category: Gorelik, A]]
	[[Category: Illes, K]]		[[Category: Illes, K]]

OCA at 05:47, 3 January 2018

OCA — Wed, 03 Jan 2018 05:47:12 GMT

←Older revision		Revision as of 05:47, 3 January 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5w7b is ~~ON HOLD until Paper Publication~~	+	==Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS==
-		+	<StructureSection load='5w7b' size='340' side='right' caption='[[5w7b]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5w7b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W7B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W7B FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PA1:2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE'>PA1</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyloxyacyl_hydrolase Acyloxyacyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.77 3.1.1.77] </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=5w7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w7b OCA], [http://pdbe.org/5w7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w7b RCSB], [http://www.ebi.ac.uk/pdbsum/5w7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w7b ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AOAH_RABIT AOAH_RABIT]] Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.[UniProtKB:O35298]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Acyloxyacyl hydrolase]]
		+	[[Category: Gorelik, A]]
		+	[[Category: Illes, K]]
		+	[[Category: Nagar, B]]
		+	[[Category: Gdsl esterase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Lipopolysaccharide]]
		+	[[Category: Lp]]
		+	[[Category: Saposin]]

OCA: Protected "5w7b" [edit=sysop:move=sysop]

OCA — Wed, 27 Sep 2017 14:31:56 GMT

Protected "5w7b" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:31, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5w7b is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 27 Sep 2017 14:31:55 GMT

New page: '''Unreleased structure''' The entry 5w7b is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5w7b is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]