4m6b

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{{STRUCTURE_4m6b| PDB=4m6b | SCENE= }}
 
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===Crystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimer===
 
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{{ABSTRACT_PUBMED_24507717}}
 
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==Function==
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==Crystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimer==
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[[http://www.uniprot.org/uniprot/H2B1_YEAST H2B1_YEAST]] 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.<ref>PMID:11973294</ref> <ref>PMID:12152067</ref> <ref>PMID:14752010</ref> <ref>PMID:15280549</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15632126</ref> <ref>PMID:15632065</ref> <ref>PMID:16598039</ref> [[http://www.uniprot.org/uniprot/SWR1_YEAST SWR1_YEAST]] Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.<ref>PMID:14690608</ref> <ref>PMID:15045029</ref> <ref>PMID:15353583</ref> <ref>PMID:14645854</ref>
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<StructureSection load='4m6b' size='340' side='right'caption='[[4m6b]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[4m6b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M6B FirstGlance]. <br>
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[[4m6b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6B OCA].
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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]] 1.78&#8491;</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=4m6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m6b OCA], [https://pdbe.org/4m6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m6b RCSB], [https://www.ebi.ac.uk/pdbsum/4m6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m6b ProSAT]</span></td></tr>
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==Reference==
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</table>
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<ref group="xtra">PMID:024507717</ref><references group="xtra"/><references/>
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== Function ==
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[[Category: DNA helicase]]
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[https://www.uniprot.org/uniprot/H2AZ_YEAST H2AZ_YEAST] Variant histone H2A which can replace H2A in some nucleosomes. 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. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received (PubMed:11000274, PubMed:11081628, PubMed:11090616, PubMed:11509669, PubMed:12628191, PubMed:14645854, PubMed:14690608, PubMed:15045029, PubMed:16239142, PubMed:16344463, PubMed:16543223). Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins (PubMed:16543222). Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes (PubMed:11509669). Involved in chromosome stability (PubMed:15353583). Required to target MPS3 to the inner membrane of the nuclear envelope (PubMed:21518795).<ref>PMID:11000274</ref> <ref>PMID:11081628</ref> <ref>PMID:11090616</ref> <ref>PMID:11509669</ref> <ref>PMID:12628191</ref> <ref>PMID:14645854</ref> <ref>PMID:14690608</ref> <ref>PMID:15045029</ref> <ref>PMID:15353583</ref> <ref>PMID:16239142</ref> <ref>PMID:16344463</ref> <ref>PMID:16543222</ref> <ref>PMID:16543223</ref> <ref>PMID:21518795</ref> [https://www.uniprot.org/uniprot/H2B1_YEAST H2B1_YEAST] 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.<ref>PMID:11973294</ref> <ref>PMID:12152067</ref> <ref>PMID:14752010</ref> <ref>PMID:15280549</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15632126</ref> <ref>PMID:15632065</ref> <ref>PMID:16598039</ref>
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[[Category: Bai, Y W.]]
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== References ==
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[[Category: Chen, J H.]]
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<references/>
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[[Category: Feng, H Q.]]
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__TOC__
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[[Category: Girlando, R.]]
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</StructureSection>
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[[Category: Hong, J J.]]
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[[Category: Large Structures]]
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[[Category: Jiang, J S.]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Ranjan, A.]]
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[[Category: Bai YW]]
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[[Category: Wang, F.]]
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[[Category: Chen JH]]
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[[Category: Wu, C.]]
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[[Category: Feng HQ]]
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[[Category: Xiao, T S.]]
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[[Category: Girlando R]]
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[[Category: Chromatin remodeler]]
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[[Category: Hong JJ]]
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[[Category: Histone binding]]
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[[Category: Jiang JS]]
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[[Category: Structural protein-hydrolase complex]]
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[[Category: Ranjan A]]
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[[Category: Wang F]]
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[[Category: Wu C]]
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[[Category: Xiao TS]]

Current revision

Crystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimer

PDB ID 4m6b

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