3QB0

Crystal structure of Actin-related protein Arp4 from S. cerevisiae complexed with ATP

3QB0 の概要

• エントリーDOI: 10.2210/pdb3qb0/pdb
• 分子名称: Actin-related protein 4, ADENOSINE-5'-TRIPHOSPHATE, CALCIUM ION (3 entities in total)
• 機能のキーワード: actin fold, atp binding, nucleus, structural protein
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Nucleus: P80428
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 226641.46

構造登録者

Fenn, S.,Breitsprecher, D.,Gerhold, C.B.,Witte, G.,Faix, J.,Hopfner, K.P. (登録日: 2011-01-12, 公開日: 2011-05-04, 最終更新日: 2023-09-13)

主引用文献

Fenn, S.,Breitsprecher, D.,Gerhold, C.B.,Witte, G.,Faix, J.,Hopfner, K.P.
Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin.
Embo J., 30:2153-2166, 2011

PubMed Abstract: Nuclear actin and actin-related proteins (Arps) are integral components of various chromatin-remodelling complexes. Actin in such nuclear assemblies does not form filaments but associates in defined complexes, for instance with Arp4 and Arp8 in the INO80 remodeller. To understand the relationship between nuclear actin and its associated Arps and to test the possibility that Arp4 and Arp8 help maintain actin in defined states, we structurally analysed Arp4 and Arp8 from Saccharomyces cerevisiae and tested their biochemical effects on actin assembly and disassembly. The solution structures of isolated Arp4 and Arp8 indicate them to be monomeric and the crystal structure of ATP-Arp4 reveals several differences to actin that explain why Arp4 does not form filaments itself. Remarkably, Arp4, assisted by Arp8, influences actin polymerization in vitro and is able to depolymerize actin filaments. Arp4 likely forms a complex with monomeric actin via the barbed end. Our data thus help explaining how nuclear actin is held in a discrete complex within the INO80 chromatin remodeller.

PubMed: 21499228
DOI: 10.1038/emboj.2011.118

実験手法

X-RAY DIFFRACTION (3.404 Å)