6ZYX

Outer Dynein Arm-Shulin complex - Shulin region from Tetrahymena thermophila

6ZYX の概要

• エントリーDOI: 10.2210/pdb6zyx/pdb
• EMDBエントリー: 11579
• 分子名称: Dynein heavy chain, outer arm protein, Flagellar outer dynein arm intermediate protein, putative, GUANOSINE-5'-TRIPHOSPHATE, ... (11 entities in total)
• 機能のキーワード: cilia, microtubules, motor, complex, motor protein
• 由来する生物種: Tetrahymena thermophila CU428; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 905944.11

構造登録者

Mali, G.R.,Abid Ali, F.,Lau, C.K.,Carter, A.P. (登録日: 2020-08-03, 公開日: 2021-01-20, 最終更新日: 2024-05-01)

主引用文献

Mali, G.R.,Ali, F.A.,Lau, C.K.,Begum, F.,Boulanger, J.,Howe, J.D.,Chen, Z.A.,Rappsilber, J.,Skehel, M.,Carter, A.P.
Shulin packages axonemal outer dynein arms for ciliary targeting.
Science, 371:910-916, 2021

PubMed Abstract: The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these ~1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate to identify two factors (Q22YU3 and Q22MS1) that bind ODAs in the cytoplasm and are required for ODA delivery to cilia. Q22YU3, which we named Shulin, locked the ODA motor domains into a closed conformation and inhibited motor activity. Cryo-electron microscopy revealed how Shulin stabilized this compact form of ODAs by binding to the dynein tails. Our findings provide a molecular explanation for how newly assembled dyneins are packaged for delivery to the cilia.

PubMed: 33632841
DOI: 10.1126/science.abe0526

実験手法

ELECTRON MICROSCOPY (4.3 Å)