3TU4

Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.

3TU4 の概要

• エントリーDOI: 10.2210/pdb3tu4/pdb
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: histones, nucleosome, gene silencing, signaling protein-structural protein-dna complex, signaling protein/structural protein/dna
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna); 詳細
• 細胞内の位置: Nucleus: P84233 P62799 P02281 3TU4; Nucleus (By similarity): Q6AZJ8
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 253414.99

構造登録者

Armache, K.-J.,Garlick, J.D.,Canzio, D.,Narlikar, G.J.,Kingston, R.E. (登録日: 2011-09-15, 公開日: 2011-11-23, 最終更新日: 2024-02-28)

主引用文献

Armache, K.J.,Garlick, J.D.,Canzio, D.,Narlikar, G.J.,Kingston, R.E.
Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution.
Science, 334:977-982, 2011

PubMed Abstract: Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.

PubMed: 22096199
DOI: 10.1126/science.1210915

実験手法

X-RAY DIFFRACTION (3 Å)