8BX8

In situ outer dynein arm from Chlamydomonas reinhardtii in the post-power stroke state

これはPDB形式変換不可エントリーです。

8BX8 の概要

• エントリーDOI: 10.2210/pdb8bx8/pdb
• EMDBエントリー: 16312
• 分子名称: Dynein heavy chain, outer arm protein, Dynein light chain, Dynein light chain tctex-type 1 protein, ... (21 entities in total)
• 機能のキーワード: axoneme, outer dynein arm, post power stroke, dynein, motor protein
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 1883795.58

構造登録者

Zimmermann, N.E.L.,Noga, A.,Obbineni, J.M.,Ishikawa, T. (登録日: 2022-12-08, 公開日: 2023-05-10, 最終更新日: 2023-06-28)

主引用文献

Zimmermann, N.,Noga, A.,Obbineni, J.M.,Ishikawa, T.
ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography.
Embo J., 42:e112466-e112466, 2023

PubMed Abstract: Axonemal outer dynein arm (ODA) motors generate force for ciliary beating. We analyzed three states of the ODA during the power stroke cycle using in situ cryo-electron tomography, subtomogram averaging, and classification. These states of force generation depict the prepower stroke, postpower stroke, and intermediate state conformations. Comparison of these conformations to published in vitro atomic structures of cytoplasmic dynein, ODA, and the Shulin-ODA complex revealed differences in the orientation and position of the dynein head. Our analysis shows that in the absence of ATP, all dynein linkers interact with the AAA3/AAA4 domains, indicating that interactions with the adjacent microtubule doublet B-tubule direct dynein orientation. For the prepower stroke conformation, there were changes in the tail that is anchored on the A-tubule. We built models starting with available high-resolution structures to generate a best-fitting model structure for the in situ pre- and postpower stroke ODA conformations, thereby showing that ODA in a complex with Shulin adopts a similar conformation as the active prepower stroke ODA in the axoneme.

PubMed: 37051721
DOI: 10.15252/embj.2022112466

実験手法

ELECTRON MICROSCOPY (30.3 Å)