2jss: Difference between revisions
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[[Image: | ==NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B== | ||
<StructureSection load='2jss' size='340' side='right' caption='[[2jss]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jss]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JSS FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yfq|1yfq]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HTB1, H2B1, SPT12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | |||
<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=2jss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jss RCSB], [http://www.ebi.ac.uk/pdbsum/2jss PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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> | |||
== 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/chain_selection.php?pdb_ID=2ata 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 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Histone|Histone]] | *[[Histone|Histone]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bai, Y | [[Category: Bai, Y]] | ||
[[Category: Feng, H | [[Category: Feng, H]] | ||
[[Category: Freedberg, D I | [[Category: Freedberg, D I]] | ||
[[Category: Hansen, D F | [[Category: Hansen, D F]] | ||
[[Category: Kato, H | [[Category: Kato, H]] | ||
[[Category: Kay, L E | [[Category: Kay, L E]] | ||
[[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-nuclear protein complex]] | ||
[[Category: Chaperone-structural protein complex]] | [[Category: Chaperone-structural protein complex]] | ||
[[Category: Histone-chaperone complex]] | [[Category: Histone-chaperone complex]] | ||
[[Category: Intrinsically unfolded protein]] | [[Category: Intrinsically unfolded protein]] | ||
Revision as of 18:45, 25 December 2014
NMR structure of chaperone Chz1 complexed with histone H2A.Z-H2B
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