6E88

Cryo-EM structure of C. elegans GDP-microtubule

6E88 の概要

• エントリーDOI: 10.2210/pdb6e88/pdb
• EMDBエントリー: 9004
• 分子名称: Tubulin alpha-2 chain, Tubulin beta-2 chain, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cytoskeletal protein, structural protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 583667.87

構造登録者

Chaaban, S.,Jariwala, S.,Chieh-Ting, H.,Redemann, S.,Kollman, J.,Muller-Reichert, T.,Sept, D.,Bui, K.H.,Brouhard, G.J. (登録日: 2018-07-27, 公開日: 2018-10-10, 最終更新日: 2024-03-13)

主引用文献

Chaaban, S.,Jariwala, S.,Hsu, C.T.,Redemann, S.,Kollman, J.M.,Muller-Reichert, T.,Sept, D.,Bui, K.H.,Brouhard, G.J.
The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth.
Dev. Cell, 47:191-, 2018

PubMed Abstract: The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what limits microtubule growth, what determines microtubule structure, or whether the mechanisms of dynamic instability are universal. Here, we studied microtubules from the nematode C. elegans, which have strikingly fast growth rates and non-canonical lattices in vivo. Using a reconstitution approach, we discovered that C. elegans microtubules combine intrinsically fast growth with very frequent catastrophes. We solved the structure of C. elegans microtubules to 4.8 Å and discovered sequence divergence in the lateral contact loops, one of which is ordered in C. elegans but unresolved in other species. We provide direct evidence that C. elegans tubulin has a higher free energy in solution and propose a model wherein the ordering of lateral contact loops activates tubulin for growth.

PubMed: 30245157
DOI: 10.1016/j.devcel.2018.08.023

実験手法

ELECTRON MICROSCOPY (4.8 Å)