3DWL

Crystal Structure of Fission Yeast Arp2/3 Complex Lacking the Arp2 Subunit

3DWL の概要

• エントリーDOI: 10.2210/pdb3dwl/pdb
• 分子名称: Actin-related protein 3, Actin-related protein 2/3 complex subunit 1, Actin-related protein 2/3 complex subunit 2, ... (7 entities in total)
• 機能のキーワード: propellor, actin-binding, atp-binding, cytoskeleton, nucleotide-binding, wd repeat, structural protein
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, actin patch: P32390 P78774 O14241 Q9Y7J4 Q92352 Q10316
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 366057.03

構造登録者

Nolen, B.J.,Pollard, T.D. (登録日: 2008-07-22, 公開日: 2008-08-26, 最終更新日: 2023-08-30)

主引用文献

Nolen, B.J.,Pollard, T.D.
Structure and biochemical properties of fission yeast arp2/3 complex lacking the arp2 subunit.
J.Biol.Chem., 283:26490-26498, 2008

PubMed Abstract: Arp2/3 (actin-related protein 2/3) complex is a seven-subunit complex that nucleates branched actin filaments in response to cellular signals. Nucleation-promoting factors such as WASp/Scar family proteins activate the complex by facilitating the activating conformational change and recruiting the first actin monomer for the daughter branch. Here we address the role of the Arp2 subunit in the function of Arp2/3 complex by isolating a version of the complex lacking Arp2 (Arp2Delta Arp2/3 complex) from fission yeast. An x-ray crystal structure of the DeltaArp2 Arp2/3 complex showed that the rest of the complex is unperturbed by the loss of Arp2. However, the Arp2Delta Arp2/3 complex was inactive in actin nucleation assays, indicating that Arp2 is essential to form a branch. A fluorescence anisotropy assay showed that Arp2 does not contribute to the affinity of the complex for Wsp1-VCA, a Schizosaccharomyces pombe nucleation-promoting factor protein. Fluorescence resonance energy transfer experiments showed that the loss of Arp2 does not prevent VCA from recruiting an actin monomer to the complex. Truncation of the N terminus of ARPC5, the smallest subunit in the complex, increased the yield of Arp2Delta Arp2/3 complex during purification but did not compromise nucleation activity of the full Arp2/3 complex.

PubMed: 18640983
DOI: 10.1074/jbc.M802607200

実験手法

X-RAY DIFFRACTION (3.78 Å)