4kud

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<StructureSection load='4kud' size='340' side='right'caption='[[4kud]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='4kud' size='340' side='right'caption='[[4kud]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[4kud]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.203&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4kui|4kui]], [[4kul|4kul]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
<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>
</table>
</table>
== Function ==
== Function ==
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[[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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[https://www.uniprot.org/uniprot/H3_YEAST H3_YEAST]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fang, Q]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: He, M]]
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[[Category: Fang Q]]
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[[Category: Ren, R]]
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[[Category: He M]]
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[[Category: Sun, Y]]
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[[Category: Ren R]]
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[[Category: Wang, H]]
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[[Category: Sun Y]]
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[[Category: Wang, M]]
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[[Category: Wang H]]
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[[Category: Xu, R M]]
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[[Category: Wang M]]
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[[Category: Yang, D]]
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[[Category: Xu RM]]
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[[Category: Yang, N]]
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[[Category: Yang D]]
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[[Category: Bah domain]]
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[[Category: Yang N]]
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[[Category: Nucleosome]]
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[[Category: Nucleus]]
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[[Category: Proteprotein-dna complex]]
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[[Category: Silencing]]
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[[Category: Structural protein-transcription-dna complex]]
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Current revision

Crystal structure of N-terminal acetylated Sir3 BAH domain D205N mutant in complex with yeast nucleosome core particle

PDB ID 4kud

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