5yje

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==Crystal structure of HIRA(644-1017)==
==Crystal structure of HIRA(644-1017)==
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<StructureSection load='5yje' size='340' side='right' caption='[[5yje]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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<StructureSection load='5yje' size='340' side='right'caption='[[5yje]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yje]] is a 3 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=5YJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YJE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yje]] is a 3 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=5YJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YJE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.45&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIRA, DGCR1, HIR, TUPLE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=5yje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yje OCA], [http://pdbe.org/5yje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yje RCSB], [http://www.ebi.ac.uk/pdbsum/5yje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yje ProSAT]</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=5yje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yje OCA], [https://pdbe.org/5yje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yje RCSB], [https://www.ebi.ac.uk/pdbsum/5yje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yje ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HIRA_HUMAN HIRA_HUMAN]] Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.<ref>PMID:12370293</ref> <ref>PMID:14718166</ref> <ref>PMID:15621527</ref>
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[https://www.uniprot.org/uniprot/HIRA_HUMAN HIRA_HUMAN] Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.<ref>PMID:12370293</ref> <ref>PMID:14718166</ref> <ref>PMID:15621527</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The HIRA histone chaperone complex deposits the histone variant H3.3 onto chromatin in a DNA synthesis-independent manner. It comprises three identified subunits, HIRA, UBN1 and CABIN1, however the functional oligomerization state of the complex has not been investigated. Here we use biochemical and crystallographic analysis to show that the HIRA subunit forms a stable homotrimer that binds two subunits of CABIN1 in vitro. A HIRA mutant that is defective in homotrimer formation interacts less efficiently with CABIN1, is not enriched at DNA damage sites upon UV irradiation and cannot rescue new H3.3 deposition in HIRA knockout cells. The structural homology with the homotrimeric replisome component Ctf4/AND-1 enables the drawing of parallels and discussion of the functional importance of the homotrimerization state of the HIRA subunit.
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Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit.,Ray-Gallet D, Ricketts MD, Sato Y, Gupta K, Boyarchuk E, Senda T, Marmorstein R, Almouzni G Nat Commun. 2018 Aug 6;9(1):3103. doi: 10.1038/s41467-018-05581-y. PMID:30082790<ref>PMID:30082790</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yje" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Sato, Y]]
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[[Category: Large Structures]]
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[[Category: Senda, M]]
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[[Category: Sato Y]]
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[[Category: Senda, T]]
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[[Category: Senda M]]
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[[Category: Gene regulation]]
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[[Category: Senda T]]
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[[Category: Histone chaperone]]
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Current revision

Crystal structure of HIRA(644-1017)

PDB ID 5yje

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