4kud

<StructureSection load='4kud' size='340' side='right'caption='[[4kud]], [[Resolution|resolution]] 3.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[4kud]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KUD FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</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=4kud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kud OCA], [https://pdbe.org/4kud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kud RCSB], [https://www.ebi.ac.uk/pdbsum/4kud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kud ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[https://www.uniprot.org/uniprot/H2B1_YEAST H2B1_YEAST]] 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.<ref>PMID:11973294</ref> <ref>PMID:12152067</ref> <ref>PMID:14752010</ref> <ref>PMID:15280549</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15632126</ref> <ref>PMID:15632065</ref> <ref>PMID:16598039</ref> [[https://www.uniprot.org/uniprot/H2A2_YEAST H2A2_YEAST]] Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.<ref>PMID:11140636</ref> <ref>PMID:15458641</ref> <ref>PMID:15610741</ref> <ref>PMID:16299494</ref>

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== Publication Abstract from PubMed ==

In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.

Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.,Yang D, Fang Q, Wang M, Ren R, Wang H, He M, Sun Y, Yang N, Xu RM Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2637. PMID:23934152<ref>PMID:23934152</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 4kud" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Fang, Q]]

[[Category: He, M]]

[[Category: Ren, R]]

[[Category: Sun, Y]]

[[Category: Wang, H]]

[[Category: Wang, M]]

[[Category: Xu, R M]]

[[Category: Yang, D]]

[[Category: Yang, N]]

[[Category: Structural protein-transcription-dna complex]]