4FFB

A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a Microtubule Polymerase

4FFB の概要

• エントリーDOI: 10.2210/pdb4ffb/pdb
• 分子名称: Tubulin alpha-1 chain, Tubulin beta chain, Protein STU2, ... (5 entities in total)
• 機能のキーワード: tubulin fold, heat repeats, cytoskeleton, microtubule, tubulin, tog domain, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P09733 P02557; Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body: P46675
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 134525.50

構造登録者

Ayaz, P.,Ye, X.,Huddleston, P.,Brautigam, C.A.,Rice, L.M. (登録日: 2012-05-31, 公開日: 2012-08-15, 最終更新日: 2023-09-13)

主引用文献

Ayaz, P.,Ye, X.,Huddleston, P.,Brautigam, C.A.,Rice, L.M.
A TOG: alpha beta-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase.
Science, 337:857-860, 2012

PubMed Abstract: Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use αβ-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast αβ-tubulin. TOG1 binds αβ-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of αβ-tubulin that cannot be incorporated into microtubules, contacting α- and β-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with αβ-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin and how they selectively recognize the growing end of the microtubule.

PubMed: 22904013
DOI: 10.1126/science.1221698

実験手法

X-RAY DIFFRACTION (2.882 Å)