6YW6

Cryo-EM structure of the ARP2/3 1B5CL isoform complex.

6YW6 の概要

• エントリーDOI: 10.2210/pdb6yw6/pdb
• EMDBエントリー: 10959
• 分子名称: Actin-related protein 3, ARPC1B, Actin-related protein 2/3 complex subunit 2, ... (8 entities in total)
• 機能のキーワード: cytoskeleton, structural protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 225885.82

構造登録者

von Loeffelholz, O.,Moores, C.,Purkiss, A. (登録日: 2020-04-29, 公開日: 2020-07-22, 最終更新日: 2025-07-02)

主引用文献

von Loeffelholz, O.,Purkiss, A.,Cao, L.,Kjaer, S.,Kogata, N.,Romet-Lemonne, G.,Way, M.,Moores, C.A.
Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.
Biol Open, 9:-, 2020

PubMed Abstract: The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 Å resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes.

PubMed: 32661131
DOI: 10.1242/bio.054304

実験手法

ELECTRON MICROSCOPY (4.2 Å)