4LD9

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

Summary for 4LD9

• Entry DOI: 10.2210/pdb4ld9/pdb
• Descriptor: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• Functional Keywords: 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, nuclear protein/transcription/dna
• Biological source: Xenopus laevis (clawed frog,common platanna,platanna); More
• Cellular location: Nucleus: P84233 P62799 P02281 P06701; Nucleus (By similarity): Q6AZJ8
• Total number of polymer chains: 12
• Total formula weight: 269078.93

Authors

Arnaudo, N.,Fernandez, I.S.,McLaughlin, S.H.,Peak-Chew, S.Y.,Rhodes, D.,Martino, F. (deposition date: 2013-06-24, release date: 2013-08-14, Last modification date: 2024-11-20)

Primary citation

Arnaudo, N.,Fernandez, I.S.,McLaughlin, S.H.,Peak-Chew, S.Y.,Rhodes, D.,Martino, F.
The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.
Nat.Struct.Mol.Biol., 20:1119-1121, 2013

PubMed Abstract: 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.

PubMed: 23934150
DOI: 10.1038/nsmb.2641

Experimental method

X-RAY DIFFRACTION (3.306 Å)