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4ld9
From Proteopedia
Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
Function
[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 Structure
4ld9 is a 12 chain structure with sequence from Saccharomyces cerevisiae s288c and Xenopus laevis. Full crystallographic information is available from OCA.
Categories: 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
