3u3d

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<StructureSection load='3u3d' size='340' side='right'caption='[[3u3d]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3u3d' size='340' side='right'caption='[[3u3d]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u3d]] 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=3U3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u3d]] 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=3U3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U3D FirstGlance]. <br>
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</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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>
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<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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u31|3u31]]</div></td></tr>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3d OCA], [https://pdbe.org/3u3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3d RCSB], [https://www.ebi.ac.uk/pdbsum/3u3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3d 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=3u3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3d OCA], [https://pdbe.org/3u3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u3d RCSB], [https://www.ebi.ac.uk/pdbsum/3u3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u3d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acyl-lysine deacylase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Plaf7]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Hao, Q]]
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[[Category: Hao Q]]
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[[Category: Zhou, Y]]
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[[Category: Zhou Y]]
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[[Category: Hydrolase]]
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[[Category: Nad-dependent deacylase]]
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[[Category: Rossmann fold domain]]
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[[Category: Zn-binding domain]]
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Current revision

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

PDB ID 3u3d

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