This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2jss
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==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
| |||||||||||
