7N32

protofilaments of microtubule doublets bound to outer-arm dynein

7N32 の概要

• エントリーDOI: 10.2210/pdb7n32/pdb
• EMDBエントリー: 22677
• 分子名称: Tubulin alpha chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: protofilament of microtubule doublet, structural protein
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1202525.56

構造登録者

Rao, Q.,Zhang, K. (登録日: 2021-05-31, 公開日: 2021-09-29, 最終更新日: 2024-05-29)

主引用文献

Rao, Q.,Han, L.,Wang, Y.,Chai, P.,Kuo, Y.W.,Yang, R.,Hu, F.,Yang, Y.,Howard, J.,Zhang, K.
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.
Nat.Struct.Mol.Biol., 28:799-810, 2021

PubMed Abstract: Thousands of outer-arm dyneins (OADs) are arrayed in the axoneme to drive a rhythmic ciliary beat. Coordination among multiple OADs is essential for generating mechanical forces to bend microtubule doublets (MTDs). Using electron microscopy, we determined high-resolution structures of Tetrahymena thermophila OAD arrays bound to MTDs in two different states. OAD preferentially binds to MTD protofilaments with a pattern resembling the native tracks for its distinct microtubule-binding domains. Upon MTD binding, free OADs are induced to adopt a stable parallel conformation, primed for array formation. Extensive tail-to-head (TTH) interactions between OADs are observed, which need to be broken for ATP turnover by the dynein motor. We propose that OADs in an array sequentially hydrolyze ATP to slide the MTDs. ATP hydrolysis in turn relaxes the TTH interfaces to effect free nucleotide cycles of downstream OADs. These findings lead to a model explaining how conformational changes in the axoneme produce coordinated action of dyneins.

PubMed: 34556869
DOI: 10.1038/s41594-021-00656-9

実験手法

ELECTRON MICROSCOPY (4.5 Å)