6VE7

The inner junction complex of Chlamydomonas reinhardtii doublet microtubule

これはPDB形式変換不可エントリーです。

6VE7 の概要

• エントリーDOI: 10.2210/pdb6ve7/pdb
• EMDBエントリー: 20858
• 分子名称: Flagellar associated protein, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (12 entities in total)
• 機能のキーワード: cilia, doublet, axoneme, microtubule inner protein, structural protein
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• タンパク質・核酸の鎖数: 62
• 化学式量合計: 2845886.26

構造登録者

Khalifa, A.A.Z.,Ichikawa, M.,Bui, K.H. (登録日: 2019-12-30, 公開日: 2020-02-05, 最終更新日: 2024-10-09)

主引用文献

Khalifa, A.A.Z.,Ichikawa, M.,Dai, D.,Kubo, S.,Black, C.,Peri, K.,McAlear, T.S.,Veyron, S.,Yang, S.K.,Vargas, J.,Bechstedt, S.,Trempe, J.F.,Bui, K.H.
The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications.
Elife, 9:-, 2020

PubMed Abstract: Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of and , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility.

PubMed: 31951202
DOI: 10.7554/eLife.52760

実験手法

ELECTRON MICROSCOPY (3.6 Å)