3u31 - Revision history

OCA at 17:34, 1 November 2023

OCA — Wed, 01 Nov 2023 17:34:46 GMT

←Older revision		Revision as of 17:34, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3u31' size='340' side='right'caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3u31' size='340' side='right'caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Plaf7 Plaf7~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U31 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE~~-~~ADENINE-DINUCLEOTIDE'>NAD</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;~~'>~~[[3u3d\|3u3d]]~~</~~div~~>~~</td></tr>~~	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152~~, ~~Sir2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Acyl-lysine_deacylase Acyl-lysine deacylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17]~~ </~~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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [https://pdbe.org/3u31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [https://www.ebi.ac.uk/pdbsum/3u31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u31 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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [https://pdbe.org/3u31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [https://www.ebi.ac.uk/pdbsum/3u31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u31 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~SIR5_PLAF7 SIR5_PLAF7]~~] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18221799</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18729382</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>	+	[https://www.uniprot.org/uniprot/SIR2A_PLAF7 SIR2A_PLAF7] NAD-dependent protein deacylase (PubMed:21992006). Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues (PubMed:21992006). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo (PubMed:17827348, PubMed:18729382, PubMed:18397290, PubMed:18221799, PubMed:20601220, PubMed:21992006). Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis (PubMed:15820676, PubMed:22379140). Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance (PubMed:19402747). Involved in recruiting ORC1 to the telomers and subtelomeric repeat regions (TAREs) and promoters of var genes (PubMed:22379140). Can ADP-ribosylate both histones and itself (PubMed:17827348). May also have a role in telomeric end protection (PubMed:18525026).<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18221799</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18729382</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref> <ref>PMID:21992006</ref> <ref>PMID:22379140</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Acyl-lysine deacylase~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Plaf7~~]]	+	[[Category: Plasmodium falciparum 3D7]]
-	[[Category: Hao, Q]]	+	[[Category: Hao Q]]
-	[[Category: Zhou, Y]]	+	[[Category: Zhou Y]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nad-dependent deacylase]]~~	+
-	~~[[Category: Nuclear]]~~	+
-	~~[[Category: Rossmann fold domain]]~~	+
-	~~[[Category: Zn-binding domain~~]]	+

OCA at 05:55, 13 July 2022

OCA — Wed, 13 Jul 2022 05:55:40 GMT

←Older revision		Revision as of 05:55, 13 July 2022
Line 1:		Line 1:

	==Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine==		==Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine==
-	<StructureSection load='3u31' size='340' side='right' caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='3u31' size='340' side='right'caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3U31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U31 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u3d\|3u3d]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Acyl-lysine_deacylase Acyl-lysine deacylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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-lysine_deacylase Acyl-lysine deacylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [~~http~~://pdbe.org/3u31 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3u31 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3u31 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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [https://pdbe.org/3u31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [https://www.ebi.ac.uk/pdbsum/3u31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u31 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SIR5_PLAF7 SIR5_PLAF7]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18221799</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18729382</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>	+	[[https://www.uniprot.org/uniprot/SIR5_PLAF7 SIR5_PLAF7]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18221799</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18729382</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Acyl-lysine deacylase]]		[[Category: Acyl-lysine deacylase]]
		+	[[Category: Large Structures]]
	[[Category: Plaf7]]		[[Category: Plaf7]]
	[[Category: Hao, Q]]		[[Category: Hao, Q]]

OCA at 05:42, 5 August 2016

OCA — Fri, 05 Aug 2016 05:42:52 GMT

←Older revision		Revision as of 05:42, 5 August 2016
Line 1:		Line 1:
		+
	==Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine==		==Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine==
	<StructureSection load='3u31' size='340' side='right' caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3u31' size='340' side='right' caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Plasmodium_falciparum Plasmodium falciparum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U31 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U31 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~5833 Plasmodium falciparum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-lysine_deacylase Acyl-lysine deacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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-lysine_deacylase Acyl-lysine deacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [http://www.ebi.ac.uk/pdbsum/3u31 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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [http://pdbe.org/3u31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [http://www.ebi.ac.uk/pdbsum/3u31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u31 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~Q8IE47_PLAF7 Q8IE47_PLAF7~~]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:~~18729382~~</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:~~18221799~~</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>	+	[[http://www.uniprot.org/uniprot/SIR5_PLAF7 SIR5_PLAF7]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18221799</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18729382</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 21:
	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 3u31" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Acyl-lysine deacylase]]		[[Category: Acyl-lysine deacylase]]
-	[[Category: ~~Plasmodium falciparum~~]]	+	[[Category: Plaf7]]
	[[Category: Hao, Q]]		[[Category: Hao, Q]]
	[[Category: Zhou, Y]]		[[Category: Zhou, Y]]

OCA at 23:29, 24 December 2014

OCA — Wed, 24 Dec 2014 23:29:53 GMT

←Older revision		Revision as of 23:29, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U31 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U31 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-lysine_deacylase Acyl-lysine deacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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-lysine_deacylase Acyl-lysine deacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [http://www.ebi.ac.uk/pdbsum/3u31 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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [http://www.ebi.ac.uk/pdbsum/3u31 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q8IE47_PLAF7 Q8IE47_PLAF7]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of medium and long chain fatty acyl groups from lysine residues. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Regulates the expression of the surface antigen-coding var genes central to the malaria pathogenesis. Cooperates with Sir2B to mediate silencing and mutual exclusive expression of only 1 of the 60 subtelomeric var genes at a time, coding for functionally different but epitopically variant versions of the erythrocyte membrane protein 1 (PfEMP1) molecule, to evade the detection by host immune surveillance. Can ADP-ribosylate both histones and itself. May also have a role in telomeric end protection.<ref>PMID:15820676</ref> <ref>PMID:17827348</ref> <ref>PMID:18729382</ref> <ref>PMID:18397290</ref> <ref>PMID:18525026</ref> <ref>PMID:18221799</ref> <ref>PMID:19402747</ref> <ref>PMID:20601220</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 18:
	Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine.,Zhu AY, Zhou Y, Khan S, Deitsch KW, Hao Q, Lin H ACS Chem Biol. 2011 Oct 21. PMID:21992006<ref>PMID:21992006</ref>		Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine.,Zhu AY, Zhou Y, Khan S, Deitsch KW, Hao Q, Lin H ACS Chem Biol. 2011 Oct 21. PMID:21992006<ref>PMID:21992006</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 ==
Line 24:		Line 26:
	[[Category: Acyl-lysine deacylase]]		[[Category: Acyl-lysine deacylase]]
	[[Category: Plasmodium falciparum]]		[[Category: Plasmodium falciparum]]
-	[[Category: Hao, Q.]]	+	[[Category: Hao, Q]]
-	[[Category: Zhou, Y.]]	+	[[Category: Zhou, Y]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Nad-dependent deacylase]]		[[Category: Nad-dependent deacylase]]

OCA at 06:05, 5 June 2014

OCA — Thu, 05 Jun 2014 06:05:39 GMT

←Older revision		Revision as of 06:05, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3u31.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine==
		+	<StructureSection load='3u31' size='340' side='right' caption='[[3u31]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U31 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u3d\|3u3d]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF13_0152, Sir2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-lysine_deacylase Acyl-lysine deacylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.17 3.5.1.17] </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=3u31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u31 RCSB], [http://www.ebi.ac.uk/pdbsum/3u31 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Plasmodium falciparum Sir2A (PfSir2A), a member of the sirtuin family of nicotinamide adenine dinucleotide-dependent deacetylases, has been shown to regulate the expression of surface antigens to evade the detection by host immune surveillance. It is thought that PfSir2A achieves this by deacetylating histones. However, the deacetylase activity of PfSir2A is weak. Here we present enzymology and structural evidence supporting that PfSir2A catalyzes the hydrolysis of medium and long chain fatty acyl groups from lysine residues more efficiently. Furthermore, P. falciparum proteins are found to contain such fatty acyl lysine modifications that can be removed by purified PfSir2A in vitro. Together, the data suggest that the physiological function of PfSir2A in antigen variation may be achieved by removing medium and long chain fatty acyl groups from protein lysine residues. The robust activity of PfSir2A would also facilitate the development of PfSir2A inhibitors, which may have therapeutic value in malaria treatment.

-	~~<!--~~	+	Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl Lysine.,Zhu AY, Zhou Y, Khan S, Deitsch KW, Hao Q, Lin H ACS Chem Biol. 2011 Oct 21. PMID:21992006<ref>PMID:21992006</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3u31"~~, ~~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_3u31\| PDB=3u31 \| SCENE= }}~~	+

-	~~===Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_21992006}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 21992006 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_21992006}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3u31]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021992006<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Acyl-lysine deacylase]]		[[Category: Acyl-lysine deacylase]]
	[[Category: Plasmodium falciparum]]		[[Category: Plasmodium falciparum]]

OCA at 11:38, 9 November 2011

OCA — Wed, 09 Nov 2011 11:38:03 GMT

←Older revision		Revision as of 11:38, 9 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3u31.jpg\|left\|200px]]

-	The ~~entry 3u31~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3u31", 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_3u31\| PDB=3u31 \| SCENE= }}

-	~~Authors: Zhou, Y., Hao, Q.~~	+	===Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine===

-	~~Description~~: Plasmodium falciparum ~~Sir2A preferentially hydrolyzes medium and long chain fatty acyl~~ lysine	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21992006}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21992006 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21992006}}
		+
		+	==About this Structure==
		+	[[3u31]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U31 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021992006</ref><references group="xtra"/>
		+	[[Category: Acyl-lysine deacylase]]
		+	[[Category: Plasmodium falciparum]]
		+	[[Category: Hao, Q.]]
		+	[[Category: Zhou, Y.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nad-dependent deacylase]]
		+	[[Category: Nuclear]]
		+	[[Category: Rossmann fold domain]]
		+	[[Category: Zn-binding domain]]

OCA: Protected "3u31" [edit=sysop:move=sysop]

OCA — Sun, 30 Oct 2011 08:49:15 GMT

Protected "3u31" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:49, 30 October 2011

OCA: New page: '''Unreleased structure''' The entry 3u31 is ON HOLD Authors: Zhou, Y., Hao, Q. Description: Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysi...

OCA — Sun, 30 Oct 2011 08:49:14 GMT

New page: '''Unreleased structure''' The entry 3u31 is ON HOLD Authors: Zhou, Y., Hao, Q. Description: Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysi...

New page

'''Unreleased structure'''

The entry 3u31 is ON HOLD

Authors: Zhou, Y., Hao, Q.

Description: Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine