View source for 4ld9


==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==
<StructureSection load='4ld9' size='340' side='right'caption='[[4ld9]], [[Resolution|resolution]] 3.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ld9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [https://pdbe.org/4ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 ProSAT]</span></td></tr>
</table>
== 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.
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== Publication Abstract from PubMed ==
The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.

The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.,Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150<ref>PMID:23934150</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ld9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Xenopus laevis]]
[[Category: Arnaudo N]]
[[Category: Fernandez IS]]
[[Category: Martino F]]
[[Category: McLaughlin SH]]
[[Category: Peak-Chew SY]]
[[Category: Rhodes D]]