7SOM

Ciliary C2 central pair apparatus isolated from Chlamydomonas reinhardtii

これはPDB形式変換不可エントリーです。

7SOM の概要

• エントリーDOI: 10.2210/pdb7som/pdb
• EMDBエントリー: 25361
• 分子名称: Tubulin beta, FAP178, Flagellar WD repeat-containing protein Pf20, ... (21 entities in total)
• 機能のキーワード: cilia, microtubule, structural protein
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• タンパク質・核酸の鎖数: 200
• 化学式量合計: 10414826.74

構造登録者

Gui, M.,Wang, X.,Dutcher, S.K.,Brown, A.,Zhang, R. (登録日: 2021-11-01, 公開日: 2022-04-13, 最終更新日: 2024-06-05)

主引用文献

Gui, M.,Wang, X.,Dutcher, S.K.,Brown, A.,Zhang, R.
Ciliary central apparatus structure reveals mechanisms of microtubule patterning.
Nat.Struct.Mol.Biol., 29:483-492, 2022

PubMed Abstract: A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules are patterned asymmetrically with large protein complexes that repeat every 16 or 32 nm. The composition of these projections and the mechanisms that establish asymmetry and longitudinal periodicity are unknown. Here, by determining cryo-EM structures of the CA microtubules, we identify 48 different CA-associated proteins, which in turn reveal mechanisms for asymmetric and periodic protein binding to microtubules. We identify arc-MIPs, a novel class of microtubule inner protein, that bind laterally across protofilaments and remodel tubulin structure and lattice contacts. The binding mechanisms utilized by CA proteins may be generalizable to other microtubule-associated proteins. These structures establish a foundation to elucidate the contributions of individual CA proteins to ciliary motility and ciliopathies.

PubMed: 35578023
DOI: 10.1038/s41594-022-00770-2

実験手法

ELECTRON MICROSCOPY (3.7 Å)