1SA0

TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX

1SA0 の概要

• エントリーDOI: 10.2210/pdb1sa0/pdb
• 関連するPDBエントリー: 1SA1
• 分子名称: Tubulin alpha chain, Tubulin beta chain, Stathmin 4, ... (7 entities in total)
• 機能のキーワード: alpha-tubulin, beta-tubulin, colchicine, gtpase, microtubule podophyllotoxin, stathmin, tubulin, cell cycle
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P02550 P02554
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 219723.88

構造登録者

Ravelli, R.B.,Gigant, B.,Curmi, P.A.,Jourdain, I.,Lachkar, S.,Sobel, A.,Knossow, M. (登録日: 2004-02-06, 公開日: 2004-03-23, 最終更新日: 2024-02-14)

主引用文献

Ravelli, R.B.,Gigant, B.,Curmi, P.A.,Jourdain, I.,Lachkar, S.,Sobel, A.,Knossow, M.
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain.
Nature, 428:198-202, 2004

PubMed Abstract: Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathmin family proteins. The way in which microtubule instability is regulated at the molecular level has remained elusive, mainly because of the lack of appropriate structural data. Here, we present the structure, at 3.5 A resolution, of tubulin in complex with colchicine and with the stathmin-like domain (SLD) of RB3. It shows the interaction of RB3-SLD with two tubulin heterodimers in a curved complex capped by the SLD amino-terminal domain, which prevents the incorporation of the complexed tubulin into microtubules. A comparison with the structure of tubulin in protofilaments shows changes in the subunits of tubulin as it switches from its straight conformation to a curved one. These changes correlate with the loss of lateral contacts and provide a rationale for the rapid microtubule depolymerization characteristic of dynamic instability. Moreover, the tubulin-colchicine complex sheds light on the mechanism of colchicine's activity: we show that colchicine binds at a location where it prevents curved tubulin from adopting a straight structure, which inhibits assembly.

PubMed: 15014504
DOI: 10.1038/nature02393

実験手法

X-RAY DIFFRACTION (3.58 Å)