6a7u
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of histone H2A.Bbd-H2B dimer== | |
| + | <StructureSection load='6a7u' size='340' side='right' caption='[[6a7u]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6a7u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A7U FirstGlance]. <br> | ||
| + | </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=6a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7u OCA], [http://pdbe.org/6a7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a7u RCSB], [http://www.ebi.ac.uk/pdbsum/6a7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/H2B2E_HUMAN H2B2E_HUMAN]] 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:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | H2A.Bbd, the most divergent histone variant among all known H2A type histones, is involved in gene transcription, spermiogenesis, DNA replication and RNA splicing. Incorporation of H2A.Bbd-H2B dimer, a fundamental unit of H2A.Bbd nucleosome, modulate structures of nucleosome or chromatin, but the underlying mechanism remains elusive. Here we determined a crystal structure of H2A.Bbd-H2B dimer at 2.6A resolution. Although the H2A.Bbd-H2B dimer structure largely resembles that of H2A-H2B, substitution of H2A alphaC helix residues by H2A.Bbd counterparts lead to the transition of a long alphaC-helix to the short 310-helix, likely owing to the rearrangement of the hydrogen-bond network. Moreover, structural comparison revealed a strikingly altered electrostatic potential surface for H2A.Bbd-H2B dimer displaying a diminished DNA binding capability. Our study provides the first high-resolution structure of histone variant H2A.Bbd and shed a light on biological function of H2A.Bbd. | ||
| - | + | Crystal structure of the histone heterodimer containing histone variant H2A.Bbd.,Dai L, Xie X, Zhou Z Biochem Biophys Res Commun. 2018 Sep 10;503(3):1786-1791. doi:, 10.1016/j.bbrc.2018.07.114. Epub 2018 Jul 29. PMID:30064909<ref>PMID:30064909</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6a7u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dai, L]] | ||
| + | [[Category: Zhou, Z]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: H2a bbd]] | ||
| + | [[Category: Histone]] | ||
| + | [[Category: Histone variant]] | ||
Revision as of 15:13, 27 February 2019
Crystal structure of histone H2A.Bbd-H2B dimer
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