4kud

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

spinqualitylabelsall models 4kud, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kud is a 12 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.203Å Ligands: AYA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H3_YEAST 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone 3D structures

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