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==NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B==
The line below this paragraph, containing "STRUCTURE_2jss", creates the "Structure Box" on the page.
<StructureSection load='2jss' size='340' side='right'caption='[[2jss]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2jss|  PDB=2jss  |  SCENE= }}
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/2jss_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jss" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2JSS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSS OCA].
*[[Histone 3D structures|Histone 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bai, Y.]]
[[Category: Bai Y]]
[[Category: Feng, H.]]
[[Category: Feng H]]
[[Category: Freedberg, D.]]
[[Category: Freedberg DI]]
[[Category: Hansen, F D.]]
[[Category: Hansen DF]]
[[Category: Kato, H.]]
[[Category: Kato H]]
[[Category: Key, L E.]]
[[Category: Kay LE]]
[[Category: Luk, E.]]
[[Category: Luk E]]
[[Category: Wu, C.]]
[[Category: Wu C]]
[[Category: Zhou, Z.]]
[[Category: Zhou Z]]
[[Category: Chaperone/nuclear protein complex]]
[[Category: Chaperone/structural protein complex]]
[[Category: Histone/chaperone complex]]
[[Category: Intrinsically unfolded protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:30:40 2008''

Latest revision as of 19:04, 29 May 2024

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

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