4ld9 | pdb_00004ld9

Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle

spinqualitylabelsall models 4ld9, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ld9 is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone 3D structures

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