2fj7
From Proteopedia
(Difference between revisions)
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<StructureSection load='2fj7' size='340' side='right'caption='[[2fj7]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='2fj7' size='340' side='right'caption='[[2fj7]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2fj7]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2fj7]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJ7 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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=2fj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fj7 OCA], [https://pdbe.org/2fj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fj7 RCSB], [https://www.ebi.ac.uk/pdbsum/2fj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fj7 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=2fj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fj7 OCA], [https://pdbe.org/2fj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fj7 RCSB], [https://www.ebi.ac.uk/pdbsum/2fj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fj7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/H32_XENLA H32_XENLA] 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=2fj7 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=2fj7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Poly(dA.dT) DNA sequence elements are thought to promote transcription by either excluding nucleosomes or by altering their structural or dynamic properties. Here, the stability and structure of a defined nucleosome core particle containing a 16 base-pair poly(dA.dT) element (A16 NCP) was investigated. The A16 NCP requires a significantly higher temperature for histone octamer sliding in vitro compared to comparable nucleosomes that do not contain a poly(dA.dT) element. Fluorescence resonance energy transfer showed that the interactions between the nucleosomal DNA ends and the histone octamer were destabilized in A16 NCP. The crystal structure of A16 NCP was determined to a resolution of 3.2 A. The overall structure was maintained except for local deviations in DNA conformation. These results are consistent with previous in vivo and in vitro observations that poly(dA.dT) elements cause only modest changes in DNA accessibility and modest increases in steady-state transcription levels. | ||
- | |||
- | Nucleosome core particles containing a poly(dA.dT) sequence element exhibit a locally distorted DNA structure.,Bao Y, White CL, Luger K J Mol Biol. 2006 Aug 25;361(4):617-24. Epub 2006 Jul 5. PMID:16860337<ref>PMID:16860337</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2fj7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Histone 3D structures|Histone 3D structures]] | *[[Histone 3D structures|Histone 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: African clawed frog]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Xenopus laevis]] |
- | [[Category: | + | [[Category: Bao Y]] |
- | [[Category: | + | [[Category: Luger K]] |
- | [[Category: | + | [[Category: White CL]] |
- | + | ||
- | + |
Current revision
Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
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