4AM7

ADP-BOUND C-TERMINAL DOMAIN OF ACTIN-RELATED PROTEIN ARP8 FROM S. CEREVISIAE

4AM7 の概要

• エントリーDOI: 10.2210/pdb4am7/pdb
• 関連するPDBエントリー: 4AM6
• EMDBエントリー: 2224 2225
• 分子名称: ACTIN-LIKE PROTEIN ARP8, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: nuclear protein, chromatin remodelling complex, atp-binding protein, nuclear actin-related protein, transcription regulation, dna repair
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 150481.34

構造登録者

Wuerges, J.,Saravanan, M.,Bose, D.,Cook, N.J.,Zhang, X.,Wigley, D.B. (登録日: 2012-03-07, 公開日: 2012-12-12, 最終更新日: 2023-12-20)

主引用文献

Saravanan, M.,Wuerges, J.,Bose, D.,Mccormack, E.A.,Cook, N.J.,Zhang, X.,Wigley, D.B.
Interactions between the Nucleosome Histone Core and Arp8 in the Ino80 Chromatin Remodeling Complex.
Proc.Natl.Acad.Sci.USA, 109:20883-, 2012

PubMed Abstract: Actin-related protein Arp8 is a component of the INO80 chromatin remodeling complex. Yeast Arp8 (yArp8) comprises two domains: a 25-KDa N-terminal domain, found only in yeast, and a 75-KDa C-terminal domain (yArp8CTD) that contains the actin fold and is conserved across other species. The crystal structure shows that yArp8CTD contains three insertions within the actin core. Using a combination of biochemistry and EM, we show that Arp8 forms a complex with nucleosomes, and that the principal interactions are via the H3 and H4 histones, mediated through one of the yArp8 insertions. We show that recombinant yArp8 exists in monomeric and dimeric states, but the dimer is the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core. Taken together, these data provide unique insight into the stoichiometry, architecture, and molecular interactions between components of the INO80 remodeling complex and nucleosomes, providing a first step toward building up the structure of the complex.

PubMed: 23213201
DOI: 10.1073/PNAS.1214735109

実験手法

X-RAY DIFFRACTION (3.25 Å)