5xm0: Difference between revisions

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 ==The mouse nucleosome structure containing H2A, H2B type3-A, H3.3, and H4==
-<StructureSection load='5xm0' size='340' side='right' caption='[[5xm0]], [[Resolution|resolution]] 2.87&Aring;' scene=''>
+<StructureSection load='5xm0' size='340' side='right'caption='[[5xm0]], [[Resolution|resolution]] 2.87&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xm0]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XM0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XM0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xm0]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XM0 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=5xm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xm0 OCA], [http://pdbe.org/5xm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xm0 RCSB], [http://www.ebi.ac.uk/pdbsum/5xm0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xm0 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.874&#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=5xm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xm0 OCA], [https://pdbe.org/5xm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xm0 RCSB], [https://www.ebi.ac.uk/pdbsum/5xm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xm0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/H2B3A_MOUSE H2B3A_MOUSE]] 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. [[http://www.uniprot.org/uniprot/H2A1B_MOUSE H2A1B_MOUSE]] 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.
+[https://www.uniprot.org/uniprot/H33_MOUSE H33_MOUSE]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Regulation of gene expression requires selective incorporation of histone H3 variant H3.3 into chromatin. Histone H3.3 has several subsidiary variants but their functions are unclear. Here we characterize the function of histone H3.3 sub-variant, H3mm7, which is expressed in skeletal muscle satellite cells. H3mm7 knockout mice demonstrate an essential role of H3mm7 in skeletal muscle regeneration. Chromatin analysis reveals that H3mm7 facilitates transcription by forming an open chromatin structure around promoter regions including those of myogenic genes. The crystal structure of the nucleosome containing H3mm7 reveals that, unlike the S57 residue of other H3 proteins, the H3mm7-specific A57 residue cannot form a hydrogen bond with the R40 residue of the cognate H4 molecule. Consequently, the H3mm7 nucleosome is unstable in vitro and exhibited higher mobility in vivo compared with the H3.3 nucleosome. We conclude that the unstable H3mm7 nucleosome may be required for proper skeletal muscle differentiation.
+Histone H3.3 sub-variant H3mm7 is required for normal skeletal muscle regeneration.,Harada A, Maehara K, Ono Y, Taguchi H, Yoshioka K, Kitajima Y, Xie Y, Sato Y, Iwasaki T, Nogami J, Okada S, Komatsu T, Semba Y, Takemoto T, Kimura H, Kurumizaka H, Ohkawa Y Nat Commun. 2018 Apr 11;9(1):1400. doi: 10.1038/s41467-018-03845-1. PMID:29643389<ref>PMID:29643389</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5xm0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone 3D structures|Histone 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Horikoshi, N]]
+[[Category: Homo sapiens]]
-[[Category: Kurumizaka, H]]
+[[Category: Large Structures]]
-[[Category: Taguchi, H]]
+[[Category: Mus musculus]]
-[[Category: Chromatin]]
+[[Category: Horikoshi N]]
-[[Category: Dna-protein complex]]
+[[Category: Kurumizaka H]]
-[[Category: Nucleosome]]
+[[Category: Taguchi H]]
-[[Category: Structural protein-dna complex]]