1Y64

Bni1p Formin Homology 2 Domain complexed with ATP-actin

1Y64 の概要

• エントリーDOI: 10.2210/pdb1y64/pdb
• 関連するPDBエントリー: 1UX4 1UX5
• 分子名称: Actin, alpha skeletal muscle, BNI1 protein, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: fh2 actin cytoskeleton, coiled coil, actin, tetramethylrhodamine-5-maleimide, atp-state, structural protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P68135; Cell membrane: P41832
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93344.85

構造登録者

Otomo, T.,Tomchick, D.R.,Otomo, C.,Panchal, S.C.,Machius, M.,Rosen, M.K. (登録日: 2004-12-03, 公開日: 2005-01-18, 最終更新日: 2011-07-13)

主引用文献

Otomo, T.,Tomchick, D.R.,Otomo, C.,Panchal, S.C.,Machius, M.,Rosen, M.K.
Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
Nature, 433:488-494, 2005

PubMed Abstract: The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.

PubMed: 15635372
DOI: 10.1038/nature03251

実験手法

X-RAY DIFFRACTION (3.05 Å)