4ld9
Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particleCrystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
Template:ABSTRACT PUBMED 23934150
FunctionFunction
[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. [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. [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. [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.
About this StructureAbout this Structure
4ld9 is a 12 chain structure with sequence from Saccharomyces cerevisiae s288c and Xenopus laevis. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F. The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150 doi:10.1038/nsmb.2641
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OCA- Saccharomyces cerevisiae s288c
- Xenopus laevis
- Arnaudo, N.
- Fernandez, I S.
- Martino, F.
- McLaughlin, S H.
- Peak-Chew, S Y.
- Rhodes, D.
- Alpha-helix
- Beta barrel
- Beta-sheet
- Chromatin
- Chromatin binding
- Double helix
- Double stranded dna
- N-terminal acetylation
- Nuclear protein-transcription-dna complex
- Nucleus
- Protein-dna complex