5W3F

Yeast tubulin polymerized with GTP in vitro

5W3F の概要

• エントリーDOI: 10.2210/pdb5w3f/pdb
• EMDBエントリー: 8755 8756 8757 8758 8759
• 分子名称: Tubulin alpha-1 chain, Tubulin beta chain, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: cytoskeleton, tubulin, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101812.01

構造登録者

Howes, S.C.,Geyer, E.A.,LaFrance, B.,Zhang, R.,Kellogg, E.H.,Westermann, S.,Rice, L.M.,Nogales, E. (登録日: 2017-06-07, 公開日: 2017-07-19, 最終更新日: 2024-03-13)

主引用文献

Howes, S.C.,Geyer, E.A.,LaFrance, B.,Zhang, R.,Kellogg, E.H.,Westermann, S.,Rice, L.M.,Nogales, E.
Structural differences between yeast and mammalian microtubules revealed by cryo-EM.
J. Cell Biol., 216:2669-2677, 2017

PubMed Abstract: Microtubules are polymers of αβ-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between αβ-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures.

PubMed: 28652389
DOI: 10.1083/jcb.201612195

実験手法

ELECTRON MICROSCOPY (3.7 Å)