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| | <StructureSection load='5bwo' size='340' side='right'caption='[[5bwo]], [[Resolution|resolution]] 2.38Å' scene=''> | | <StructureSection load='5bwo' size='340' side='right'caption='[[5bwo]], [[Resolution|resolution]] 2.38Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bwo]] is a 2 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=5BWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BWO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bwo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BWO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=PLM:PALMITIC+ACID'>PLM</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">[[5bwl|5bwl]], [[5bwn|5bwn]], [[5bwp|5bwp]], [[5bwq|5bwq]]</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=5bwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwo OCA], [https://pdbe.org/5bwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bwo RCSB], [https://www.ebi.ac.uk/pdbsum/5bwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwo ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIRT3, SIR2L3 ([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=5bwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwo OCA], [http://pdbe.org/5bwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bwo RCSB], [http://www.ebi.ac.uk/pdbsum/5bwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIR3_HUMAN SIR3_HUMAN]] NAD-dependent protein deacetylase. Activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.<ref>PMID:16788062</ref> <ref>PMID:18680753</ref> <ref>PMID:18794531</ref> <ref>PMID:19535340</ref> | + | [https://www.uniprot.org/uniprot/H3C_HUMAN H3C_HUMAN] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes.<ref>PMID:21274551</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> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gai, W]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Jiang, H]] | + | [[Category: Gai W]] |
| - | [[Category: Liu, D]] | + | [[Category: Jiang H]] |
| - | [[Category: Hydrolase]] | + | [[Category: Liu D]] |
| - | [[Category: Peptide-hydrolase complex]]
| + | |
| Structural highlights
Function
H3C_HUMAN Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes.[1]
Publication Abstract from PubMed
SIRT1-7 play important roles in many biological processes and age-related diseases. In addition to a NAD(+) -dependent deacetylase activity, they can catalyze several other reactions, including the hydrolysis of long-chain fatty acyl lysine. To study the binding modes of sirtuins to long-chain acyl lysines, we solved the crystal structures of SIRT3 bound to either a H3K9-myristoylated- or a H3K9-palmitoylated peptide. Interaction of SIRT3 with the palmitoyl group led to unfolding of the alpha3-helix. The myristoyl and palmitoyl groups bind to the C-pocket and an allosteric site near the alpha3-helix, respectively. We found that the residues preceding the alpha3-helix determine the size of the C-pocket. The flexibility of the alpha2-alpha3 loop and the plasticity of the alpha3-helix affect the interaction with long-chain acyl lysine.
Crystal structures of SIRT3 reveal that the alpha2-alpha3 loop and alpha3-helix affect the interaction with long-chain acyl lysine.,Gai W, Li H, Jiang H, Long Y, Liu D FEBS Lett. 2016 Sep;590(17):3019-28. doi: 10.1002/1873-3468.12345. Epub 2016 Aug , 24. PMID:27501476[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schenk R, Jenke A, Zilbauer M, Wirth S, Postberg J. H3.5 is a novel hominid-specific histone H3 variant that is specifically expressed in the seminiferous tubules of human testes. Chromosoma. 2011 Jun;120(3):275-85. doi: 10.1007/s00412-011-0310-4. Epub 2011 Jan, 28. PMID:21274551 doi:10.1007/s00412-011-0310-4
- ↑ Gai W, Li H, Jiang H, Long Y, Liu D. Crystal structures of SIRT3 reveal that the alpha2-alpha3 loop and alpha3-helix affect the interaction with long-chain acyl lysine. FEBS Lett. 2016 Sep;590(17):3019-28. doi: 10.1002/1873-3468.12345. Epub 2016 Aug , 24. PMID:27501476 doi:http://dx.doi.org/10.1002/1873-3468.12345
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