8SF7

48-nm doublet microtubule from Tetrahymena thermophila strain MEC17

これはPDB形式変換不可エントリーです。

8SF7 の概要

• エントリーDOI: 10.2210/pdb8sf7/pdb
• 関連するPDBエントリー: 8G2Z 8G3D
• EMDBエントリー: 29666 29667 29685 29692 29693 40436
• 分子名称: Nebulin, CFAP161A, CFAP20, ... (48 entities in total)
• 機能のキーワード: cilia, axoneme, doublet microtubule, microtubule inner protein, structural protein
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 431
• 化学式量合計: 20338705.62

構造登録者

Black, C.S.,Kubo, S.,Yang, S.K.,Bui, K.H. (登録日: 2023-04-10, 公開日: 2024-05-22, 最終更新日: 2024-10-09)

主引用文献

Yang, S.K.,Kubo, S.,Black, C.S.,Peri, K.,Dai, D.,Legal, T.,Valente-Paterno, M.,Gaertig, J.,Bui, K.H.
Effect of alpha-tubulin acetylation on the doublet microtubule structure.
Elife, 12:-, 2024

PubMed Abstract: Acetylation of α-tubulin at the lysine 40 residue (αK40) by αTAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that acetylated microtubules are more stable and damage resistant. αK40 acetylation is the only known microtubule luminal post-translational modification site. The luminal location suggests that the modification tunes the lateral interaction of protofilaments inside the microtubule. In this study, we examined the effect of tubulin acetylation on the doublet microtubule (DMT) in the cilia of using a combination of cryo-electron microscopy, molecular dynamics, and mass spectrometry. We found that αK40 acetylation exerts a small-scale effect on the DMT structure and stability by influencing the lateral rotational angle. In addition, comparative mass spectrometry revealed a link between αK40 acetylation and phosphorylation in cilia.

PubMed: 38598282
DOI: 10.7554/eLife.92219

実験手法

ELECTRON MICROSCOPY (4.1 Å)