2rvq: Difference between revisions

Revision as of 20:54, 12 April 2023

Solution structure of the isolated histone H2A-H2B heterodimer

Structural highlights

2rvq is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H2A1B_HUMAN

Publication Abstract from PubMed

During chromatin-regulated processes, the histone H2A-H2B heterodimer functions dynamically in and out of the nucleosome. Although detailed crystal structures of nucleosomes have been established, that of the isolated full-length H2A-H2B heterodimer has remained elusive. Here, we have determined the solution structure of human H2A-H2B by NMR coupled with CS-Rosetta. H2A and H2B each contain a histone fold, comprising four alpha-helices and two beta-strands (alpha1-beta1-alpha2-beta2-alpha3-alphaC), together with the long disordered N- and C-terminal H2A tails and the long N-terminal H2B tail. The N-terminal alphaN helix, C-terminal beta3 strand, and 310 helix of H2A observed in the H2A-H2B nucleosome structure are disordered in isolated H2A-H2B. In addition, the H2A alpha1 and H2B alphaC helices are not well fixed in the heterodimer, and the H2A and H2B tails are not completely random coils. Comparison of hydrogen-deuterium exchange, fast hydrogen exchange, and {(1)H}-(15)N hetero-nuclear NOE data with the CS-Rosetta structure indicates that there is some conformation in the H2A 310 helical and H2B Lys11 regions, while the repression domain of H2B (residues 27-34) exhibits an extended string-like structure. This first structure of the isolated H2A-H2B heterodimer provides insight into its dynamic functions in chromatin.

Solution structure of the isolated histone H2A-H2B heterodimer.,Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y Sci Rep. 2016 May 16;6:24999. doi: 10.1038/srep24999. PMID:27181506^[1]

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

References

↑ Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. Solution structure of the isolated histone H2A-H2B heterodimer. Sci Rep. 2016 May 16;6:24999. doi: 10.1038/srep24999. PMID:27181506 doi:https://dx.doi.org/10.1038/srep24999

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. Solution structure of the isolated histone H2A-H2B heterodimer. Sci Rep. 2016 May 16;6:24999. doi: 10.1038/srep24999. PMID:27181506 doi:https://dx.doi.org/10.1038/srep24999

[1]

@@ Line 1: / Line 1: @@
 ==Solution structure of the isolated histone H2A-H2B heterodimer==
-<StructureSection load='2rvq' size='340' side='right'caption='[[2rvq]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2rvq' size='340' side='right'caption='[[2rvq]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RVQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RVQ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIST1H2AB, H2AFM, HIST1H2AE, H2AFA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H2BJ, H2BFR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=2rvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvq OCA], [https://pdbe.org/2rvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvq RCSB], [https://www.ebi.ac.uk/pdbsum/2rvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvq ProSAT]</span></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=2rvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvq OCA], [https://pdbe.org/2rvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvq RCSB], [https://www.ebi.ac.uk/pdbsum/2rvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_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/H2A1B_HUMAN H2A1B_HUMAN]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ikeguchi, M]]
+[[Category: Ikeguchi M]]
-[[Category: Kurita, J]]
+[[Category: Kurita J]]
-[[Category: Moriwaki, Y]]
+[[Category: Moriwaki Y]]
-[[Category: Nagadoi, A]]
+[[Category: Nagadoi A]]
-[[Category: Nishimura, Y]]
+[[Category: Nishimura Y]]
-[[Category: Ohtomo, H]]
+[[Category: Ohtomo H]]
-[[Category: Sato, M]]
+[[Category: Sato M]]
-[[Category: Shimojo, H]]
+[[Category: Shimojo H]]
-[[Category: Yamane, T]]
+[[Category: Yamane T]]
-[[Category: Cs-rosetta]]
-[[Category: Dna binding protein]]
-[[Category: H2a]]
-[[Category: H2b]]
-[[Category: Histone]]
-[[Category: Nuclear protein-nuclear protein complex]]
-[[Category: Nucleosome]]

2rvq: Difference between revisions

Revision as of 20:54, 12 April 2023

Solution structure of the isolated histone H2A-H2B heterodimer

Structural highlights

Function

Publication Abstract from PubMed

References

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