7Q8C

Leishmania major actin filament in ADP-state

7Q8C の概要

• エントリーDOI: 10.2210/pdb7q8c/pdb
• 関連するPDBエントリー: 7Q8B
• EMDBエントリー: 13863 13864
• 分子名称: Actin, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: actin, filament, parasite, adp-pi, structural protein
• 由来する生物種: Leishmania major
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 212576.86

構造登録者

Kotila, T.,Muniyandi, S.,Lappalainen, P.,Huiskonen, J.T. (登録日: 2021-11-11, 公開日: 2022-05-18, 最終更新日: 2024-07-17)

主引用文献

Kotila, T.,Wioland, H.,Selvaraj, M.,Kogan, K.,Antenucci, L.,Jegou, A.,Huiskonen, J.T.,Romet-Lemonne, G.,Lappalainen, P.
Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.
Nat Commun, 13:3442-3442, 2022

PubMed Abstract: Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same overall fold and co-polymerize with each other. Interestingly, Leishmania harbors a simple actin-regulatory machinery that lacks cofilin 'cofactors', which accelerate filament disassembly in higher eukaryotes. By applying single-filament biochemistry we discovered that, compared to mammalian proteins, Leishmania actin filaments depolymerize more rapidly from both ends, and are severed > 100-fold more efficiently by cofilin. Our high-resolution cryo-EM structures of Leishmania ADP-, ADP-Pi- and cofilin-actin filaments identify specific features at actin subunit interfaces and cofilin-actin interactions that explain the unusually rapid dynamics of parasite actin filaments. Our findings reveal how divergent parasites achieve rapid actin dynamics using a remarkably simple set of actin-binding proteins, and elucidate evolution of the actin cytoskeleton.

PubMed: 35705539
DOI: 10.1038/s41467-022-31068-y

実験手法

ELECTRON MICROSCOPY (2.72 Å)