6W17

Structure of Dip1-activated Arp2/3 complex with nucleated actin filament

6W17 の概要

• エントリーDOI: 10.2210/pdb6w17/pdb
• EMDBエントリー: 21502 21503
• 分子名称: Actin-related protein 3, Phalloidin, MAGNESIUM ION, ... (13 entities in total)
• 機能のキーワード: arp2/3, actin, dip1, cytoskeletal protein, actin regulator, structural protein
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 445876.61

構造登録者

Shaaban, M.,Nolen, B.J.,Chowdhury, S. (登録日: 2020-03-03, 公開日: 2020-08-12, 最終更新日: 2025-04-02)

主引用文献

Shaaban, M.,Chowdhury, S.,Nolen, B.J.
Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.
Nat.Struct.Mol.Biol., 27:1009-1016, 2020

PubMed Abstract: Arp2/3 complex, a crucial actin filament nucleator, undergoes structural rearrangements during activation by nucleation-promoting factors (NPFs). However, the conformational pathway leading to the nucleation-competent state is unclear due to lack of high-resolution structures of the activated state. Here we report a ~3.9 Å resolution cryo-EM structure of activated Schizosaccharomyces pombe Arp2/3 complex bound to the S. pombe NPF Dip1 and attached to the end of the nucleated actin filament. The structure reveals global and local conformational changes that allow the two actin-related proteins in Arp2/3 complex to mimic a filamentous actin dimer and template nucleation. Activation occurs through a clamp-twisting mechanism, in which Dip1 forces two core subunits in Arp2/3 complex to pivot around one another, shifting half of the complex into a new activated position. By showing how Dip1 stimulates activation, the structure reveals how NPFs can activate Arp2/3 complex in diverse cellular processes.

PubMed: 32839613
DOI: 10.1038/s41594-020-0481-x

実験手法

ELECTRON MICROSCOPY (3.9 Å)