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2jss

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==NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B==
==NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B==
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<StructureSection load='2jss' size='340' side='right'caption='[[2jss]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2jss' size='340' side='right'caption='[[2jss]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2jss]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2jss]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yfq|1yfq]]</div></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">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HTB1, H2B1, SPT12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=2jss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jss OCA], [https://pdbe.org/2jss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jss RCSB], [https://www.ebi.ac.uk/pdbsum/2jss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jss 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=2jss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jss OCA], [https://pdbe.org/2jss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jss RCSB], [https://www.ebi.ac.uk/pdbsum/2jss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jss ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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> [[https://www.uniprot.org/uniprot/CHZ1_YEAST CHZ1_YEAST]] Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin.<ref>PMID:17289584</ref>
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Bai, Y]]
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[[Category: Bai Y]]
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[[Category: Feng, H]]
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[[Category: Feng H]]
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[[Category: Freedberg, D I]]
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[[Category: Freedberg DI]]
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[[Category: Hansen, D F]]
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[[Category: Hansen DF]]
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[[Category: Kato, H]]
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[[Category: Kato H]]
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[[Category: Kay, L E]]
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[[Category: Kay LE]]
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[[Category: Luk, E]]
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[[Category: Luk E]]
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[[Category: Wu, C]]
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[[Category: Wu C]]
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[[Category: Zhou, Z]]
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[[Category: Zhou Z]]
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[[Category: Chaperone-nuclear protein complex]]
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[[Category: Chaperone-structural protein complex]]
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[[Category: Histone-chaperone complex]]
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[[Category: Intrinsically unfolded protein]]
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Current revision

NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B

PDB ID 2jss

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