3c9k

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Current revision (14:04, 13 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3c9k]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9K FirstGlance]. <br>
<table><tr><td colspan='2'>[[3c9k]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9K FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hio|2hio]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20&#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=3c9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9k OCA], [https://pdbe.org/3c9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9k RCSB], [https://www.ebi.ac.uk/pdbsum/3c9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9k 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=3c9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9k OCA], [https://pdbe.org/3c9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9k RCSB], [https://www.ebi.ac.uk/pdbsum/3c9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9k ProSAT]</span></td></tr>
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</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/H4_CHICK H4_CHICK]] 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/H2A4_CHICK H2A4_CHICK]] 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/H32_CHICK H32_CHICK]] 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/H2B7_CHICK H2B7_CHICK]] 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.
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[https://www.uniprot.org/uniprot/H2A4_CHICK H2A4_CHICK] 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=3c9k ConSurf].
</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/main_output.php?pdb_ID=3c9k ConSurf].
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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A major question in chromatin involves the exact organization of nucleosomes within the 30-nm chromatin fiber and its structural determinants of assembly. Here we investigate the structure of histone octamer helical tubes via the method of iterative helical real-space reconstruction. Accurate placement of the x-ray structure of the histone octamer within the reconstructed density yields a pseudoatomic model for the entire helix, and allows precise identification of molecular interactions between neighboring octamers. One such interaction that would not be obscured by DNA in the nucleosome consists of a twofold symmetric four-helix bundle formed between pairs of H2B-alpha3 and H2B-alphaC helices of neighboring octamers. We believe that this interface can act as an internucleosomal four-helix bundle within the context of the chromatin fiber. The potential relevance of this interface in the folding of the 30-nm chromatin fiber is discussed.
 
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Histone octamer helical tubes suggest that an internucleosomal four-helix bundle stabilizes the chromatin fiber.,Frouws TD, Patterton HG, Sewell BT Biophys J. 2009 Apr 22;96(8):3363-71. PMID:19383479<ref>PMID:19383479</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3c9k" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Histone 3D structures|Histone 3D structures]]
*[[Histone 3D structures|Histone 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Frouws, T D]]
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[[Category: Frouws TD]]
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[[Category: Chromosomal protein]]
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[[Category: Dna binding protein]]
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[[Category: Helix]]
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[[Category: Methylation]]
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[[Category: Nucleosome core]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Tubular crystal]]
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Current revision

Model of Histone Octamer Tubular Crystals

3c9k, resolution 20.00Å

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