6O2S

Deacetylated Microtubules

これはPDB形式変換不可エントリーです。

6O2S の概要

• エントリーDOI: 10.2210/pdb6o2s/pdb
• EMDBエントリー: 0612 0613 0614 0615
• 分子名称: Tubulin alpha-1B chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: microtubule, cytoskeleton, acetylation, structural protein
• 由来する生物種: Sus scrofa (Pig); 詳細
• タンパク質・核酸の鎖数: 104
• 化学式量合計: 5257350.85

構造登録者

Eshun-Wilson, L.,Zhang, R.,Portran, D.,Nachury, M.V.,Toso, D.,Lohr, T.,Vendruscolo, M.,Bonomi, M.,Fraser, J.S.,Nogales, E. (登録日: 2019-02-24, 公開日: 2019-05-22, 最終更新日: 2024-03-20)

主引用文献

Eshun-Wilson, L.,Zhang, R.,Portran, D.,Nachury, M.V.,Toso, D.B.,Lohr, T.,Vendruscolo, M.,Bonomi, M.,Fraser, J.S.,Nogales, E.
Effects of alpha-tubulin acetylation on microtubule structure and stability.
Proc.Natl.Acad.Sci.USA, 116:10366-10371, 2019

PubMed Abstract: Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and acetylated states by using the experimental cryo-EM density as a structural restraint in molecular dynamics simulations. We found that acetylation alters the conformational landscape of the flexible loop that contains αK40. Modification of αK40 reduces the disorder of the loop and restricts the states that it samples. We propose that the change in conformational sampling that we describe, at a location very close to the lateral contacts site, is likely to affect microtubule stability and function.

PubMed: 31072936
DOI: 10.1073/pnas.1900441116

実験手法

ELECTRON MICROSCOPY (4 Å)