3J6F

Minimized average structure of GDP-bound dynamic microtubules

3J6F の概要

• エントリーDOI: 10.2210/pdb3j6f/pdb
• 関連するPDBエントリー: 3J6E 3J6G
• EMDBエントリー: 5895 5896 5897 5898 5899
• 分子名称: Tubulin alpha-1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: microtubule, gdp, dynamic, structural protein
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 879314.57

構造登録者

Alushin, G.M.,Lander, G.C.,Kellogg, E.H.,Zhang, R.,Baker, D.,Nogales, E. (登録日: 2014-02-19, 公開日: 2014-06-04, 最終更新日: 2024-11-06)

主引用文献

Alushin, G.M.,Lander, G.C.,Kellogg, E.H.,Zhang, R.,Baker, D.,Nogales, E.
High-Resolution Microtubule Structures Reveal the Structural Transitions in alpha beta-Tubulin upon GTP Hydrolysis.
Cell(Cambridge,Mass.), 157:1117-1129, 2014

PubMed Abstract: Dynamic instability, the stochastic switching between growth and shrinkage, is essential for microtubule function. This behavior is driven by GTP hydrolysis in the microtubule lattice and is inhibited by anticancer agents like Taxol. We provide insight into the mechanism of dynamic instability, based on high-resolution cryo-EM structures (4.7-5.6 Å) of dynamic microtubules and microtubules stabilized by GMPCPP or Taxol. We infer that hydrolysis leads to a compaction around the E-site nucleotide at longitudinal interfaces, as well as movement of the α-tubulin intermediate domain and H7 helix. Displacement of the C-terminal helices in both α- and β-tubulin subunits suggests an effect on interactions with binding partners that contact this region. Taxol inhibits most of these conformational changes, allosterically inducing a GMPCPP-like state. Lateral interactions are similar in all conditions we examined, suggesting that microtubule lattice stability is primarily modulated at longitudinal interfaces.

PubMed: 24855948
DOI: 10.1016/j.cell.2014.03.053

実験手法

ELECTRON MICROSCOPY (4.9 Å)