5f99: Difference between revisions

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'''Unreleased structure'''
==X-ray Structure of the MMTV-A Nucleosome Core Particle==
<StructureSection load='5f99' size='340' side='right' caption='[[5f99]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5f99]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F99 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5f99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f99 OCA], [http://pdbe.org/5f99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f99 RCSB], [http://www.ebi.ac.uk/pdbsum/5f99 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_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. [[http://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. [[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_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. [[http://www.uniprot.org/uniprot/H4_XENLA H4_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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The conformation of DNA bound in nucleosomes depends on the DNA sequence. Questions such as how nucleosomes are positioned and how they potentially bind sequence-dependent nuclear factors require near-atomic resolution structures of the nucleosome core containing different DNA sequences; despite this, only the DNA for two similar alpha-satellite sequences and a sequence (601) selected in vitro have been visualized bound in the nucleosome core. Here we report the 2.6-A resolution X-ray structure of a nucleosome core particle containing the DNA sequence of nucleosome A of the 3'-LTR of the mouse mammary tumor virus (147 bp MMTV-A). To our knowledge, this is the first nucleosome core particle structure containing a promoter sequence and crystallized from Mg2+ ions. It reveals sequence-dependent DNA conformations not seen previously, including kinking into the DNA major groove.


The entry 5f99 is ON HOLD
X-ray structure of the MMTV-A nucleosome core.,Frouws TD, Duda SC, Richmond TJ Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201524607. PMID:26787910<ref>PMID:26787910</ref>


Authors: Frouws, T.D., Richmond, T.J.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: X-ray Structure of the MMTV-A Nucleosome Core Particle
<div class="pdbe-citations 5f99" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Richmond, T.J]]
<references/>
[[Category: Frouws, T.D]]
__TOC__
</StructureSection>
[[Category: Frouws, T D]]
[[Category: Richmond, T J]]
[[Category: Dna binding protein]]
[[Category: Nucleosome core particle histone dna]]

Revision as of 15:42, 3 February 2016

X-ray Structure of the MMTV-A Nucleosome Core Particle

5f99, resolution 2.63Å

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