6S9E

Tubulin-GDP.AlF complex

6S9E の概要

• エントリーDOI: 10.2210/pdb6s9e/pdb
• 分子名称: Tubulin alpha-1B chain, GUANOSINE-5'-DIPHOSPHATE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (15 entities in total)
• 機能のキーワード: tubulin, cytoskeleton, gtpase, transitional state, cell cycle
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 267326.54

構造登録者

Oliva, M.A.,Estevez-Gallego, J.,Diaz, J.F.,Prota, A.E.,Steinmetz, M.O.,Balaguer, F.A.,Lucena-Agell, D. (登録日: 2019-07-12, 公開日: 2020-02-19, 最終更新日: 2024-01-24)

主引用文献

Estevez-Gallego, J.,Josa-Prado, F.,Ku, S.,Buey, R.M.,Balaguer, F.A.,Prota, A.E.,Lucena-Agell, D.,Kamma-Lorger, C.,Yagi, T.,Iwamoto, H.,Duchesne, L.,Barasoain, I.,Steinmetz, M.O.,Chretien, D.,Kamimura, S.,Diaz, J.F.,Oliva, M.A.
Structural model for differential cap maturation at growing microtubule ends.
Elife, 9:-, 2020

PubMed Abstract: Microtubules (MTs) are hollow cylinders made of tubulin, a GTPase responsible for essential functions during cell growth and division, and thus, key target for anti-tumor drugs. In MTs, GTP hydrolysis triggers structural changes in the lattice, which are responsible for interaction with regulatory factors. The stabilizing GTP-cap is a hallmark of MTs and the mechanism of the chemical-structural link between the GTP hydrolysis site and the MT lattice is a matter of debate. We have analyzed the structure of tubulin and MTs assembled in the presence of fluoride salts that mimic the GTP-bound and GDP•P transition states. Our results challenge current models because tubulin does not change axial length upon GTP hydrolysis. Moreover, analysis of the structure of MTs assembled in the presence of several nucleotide analogues and of taxol allows us to propose that previously described lattice expansion could be a post-hydrolysis stage involved in P release.

PubMed: 32151315
DOI: 10.7554/eLife.50155

実験手法

X-RAY DIFFRACTION (2.25 Å)