9MFW

Motor domain with ADP AAA1 and ADP AAA3 from yeast full-length dynein-1 in 0.1 mM ATP condition

これはPDB形式変換不可エントリーです。

9MFW の概要

• エントリーDOI: 10.2210/pdb9mfw/pdb
• EMDBエントリー: 48240
• 分子名称: Dynein heavy chain, cytoplasmic, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: dynein, motor protein
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 473707.53

構造登録者

Geohring, I.C.,Chai, P.,Iyer, B.R. (登録日: 2024-12-10, 公開日: 2025-12-17, 最終更新日: 2026-04-08)

主引用文献

Geohring, I.C.,Chai, P.,Iyer, B.R.,Ton, W.D.,Yang, J.,Ide, A.H.,George, S.C.,Bagri, J.S.,Baird, S.V.,Zhang, K.,Markus, S.M.
A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.
Nat.Chem.Biol., 22:649-662, 2026

PubMed Abstract: Dynein-1 is a microtubule motor that transports numerous cytoplasmic cargoes. Activation of motility requires it first overcome an autoinhibited state before its assembly with dynactin and a cargo adaptor. Studies suggest that Lis1 may relieve dynein's autoinhibited state, although evidence for this is lacking. We first determined the rules governing dynein-Lis1 binding, revealing that their binding affinity is regulated by the nucleotide-bound states of each of three nucleotide-binding pockets within dynein. We also found that distinct nucleotide 'codes' coordinate their binding stoichiometry by impacting binding affinity at two different sites within the dynein motor domain. Electron microscopy revealed that a 1 dynein:1 Lis1 complex directly promotes an uninhibited conformational state of dynein, whereas a 1:2 complex resembles the autoinhibited state. Cryo-electron microscopy revealed that the structural basis for Lis1 opening dynein relies on interactions with the linker domain. Our work reveals the biochemical basis by which Lis1 relieves dynein autoinhibition.

PubMed: 41571912
DOI: 10.1038/s41589-025-02096-8

実験手法

ELECTRON MICROSCOPY (4.1 Å)