7MOQ

The structure of the Tetrahymena thermophila outer dynein arm on doublet microtubule

これはPDB形式変換不可エントリーです。

7MOQ の概要

• エントリーDOI: 10.2210/pdb7moq/pdb
• EMDBエントリー: 23926
• 分子名称: Dynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative, Dynein light chain, Dynein light chain 2A, ... (27 entities in total)
• 機能のキーワード: cilia, doublet, axoneme, outer dynein arm, dynein, structural protein
• 由来する生物種: Tetrahymena thermophila CU428; 詳細
• タンパク質・核酸の鎖数: 35
• 化学式量合計: 2783901.16

構造登録者

Kubo, S.,Yang, S.K.,Ichikawa, M.,Bui, K.H. (登録日: 2021-05-03, 公開日: 2021-07-14, 最終更新日: 2024-05-29)

主引用文献

Kubo, S.,Yang, S.K.,Black, C.S.,Dai, D.,Valente-Paterno, M.,Gaertig, J.,Ichikawa, M.,Bui, K.H.
Remodeling and activation mechanisms of outer arm dyneins revealed by cryo-EM.
Embo Rep., 22:e52911-e52911, 2021

PubMed Abstract: Cilia are thin microtubule-based protrusions of eukaryotic cells. The swimming of ciliated protists and sperm cells is propelled by the beating of cilia. Cilia propagate the flow of mucus in the trachea and protect the human body from viral infections. The main force generators of ciliary beating are the outer dynein arms (ODAs) which attach to the doublet microtubules. The bending of cilia is driven by the ODAs' conformational changes caused by ATP hydrolysis. Here, we report the native ODA complex structure attaching to the doublet microtubule by cryo-electron microscopy. The structure reveals how the ODA complex is attached to the doublet microtubule via the docking complex in its native state. Combined with coarse-grained molecular dynamic simulations, we present a model of how the attachment of the ODA to the doublet microtubule induces remodeling and activation of the ODA complex.

PubMed: 34338432
DOI: 10.15252/embr.202152911

実験手法

ELECTRON MICROSCOPY (8 Å)