6a7u: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6a7u is ~~ON HOLD until Paper~~ Publication

==Crystal structure of histone H2A.Bbd-H2B dimer==

== Structural highlights ==

<table><tr><td colspan='2'>[[6a7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6A7U FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7u OCA], [https://pdbe.org/6a7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a7u RCSB], [https://www.ebi.ac.uk/pdbsum/6a7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7u ProSAT]</span></td></tr>

</table>

== Function ==

[https://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> [https://www.uniprot.org/uniprot/H2AB2_HUMAN H2AB2_HUMAN]

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Dai L]]

[[Category: Zhou Z]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6a7u is ON HOLD  until Paper Publication
+==Crystal structure of histone H2A.Bbd-H2B dimer==
+<StructureSection load='6a7u' size='340' side='right'caption='[[6a7u]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6a7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6A7U FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7u OCA], [https://pdbe.org/6a7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a7u RCSB], [https://www.ebi.ac.uk/pdbsum/6a7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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> [https://www.uniprot.org/uniprot/H2AB2_HUMAN H2AB2_HUMAN]
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6a7u" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Dai L]]
+[[Category: Zhou Z]]