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TitleThe N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 20, Page 1119-1121, Year 2013
Publish dateJun 24, 2013 (structure data deposition date)
AuthorsArnaudo, N. / Fernandez, I.S. / McLaughlin, S.H. / Peak-Chew, S.Y. / Rhodes, D. / Martino, F.
External linksNat. Struct. Mol. Biol. / PubMed:23934150
MethodsX-ray diffraction
Resolution3.306 Å
Structure data

PDB-4ld9:
Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
Method: X-RAY DIFFRACTION / Resolution: 3.306 Å

Source
  • xenopus laevis (African clawed frog)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsNUCLEAR PROTEIN/TRANSCRIPTION/DNA / BETA BARREL / PROTEIN-DNA COMPLEX / DOUBLE HELIX / alpha-helix / beta-sheet / double stranded DNA / chromatin binding / chromatin / N-terminal acetylation / nucleus / NUCLEAR PROTEIN-TRANSCRIPTION-DNA complex

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