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2jss

From Proteopedia

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{{Seed}}
 
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[[Image:2jss.png|left|200px]]
 
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<!--
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==NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B==
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The line below this paragraph, containing "STRUCTURE_2jss", creates the "Structure Box" on the page.
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<StructureSection load='2jss' size='340' side='right'caption='[[2jss]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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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or leave the SCENE parameter empty for the default display.
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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='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>
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{{STRUCTURE_2jss| PDB=2jss | SCENE= }}
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/2jss_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jss ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The NMR structure of budding yeast chaperone Chz1 complexed with histones H2A.Z-H2B has been determined. Chz1 forms a long irregular chain capped by two short alpha-helices, and uses both positively and negatively charged residues to stabilize the histone dimer. A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions.
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===NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B===
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NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.,Zhou Z, Feng H, Hansen DF, Kato H, Luk E, Freedberg DI, Kay LE, Wu C, Bai Y Nat Struct Mol Biol. 2008 Aug;15(8):868-9. Epub 2008 Jul 20. PMID:18641662<ref>PMID:18641662</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 2jss" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18641662}}, adds the Publication Abstract to the page
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*[[Histone 3D structures|Histone 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18641662 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18641662}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2JSS is a 2 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:18641662</ref><references group="xtra"/>
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:54:16 2009''
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Current revision

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

PDB ID 2jss

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