6S9E

Tubulin-GDP.AlF complex

Summary for 6S9E

• Entry DOI: 10.2210/pdb6s9e/pdb
• Descriptor: Tubulin alpha-1B chain, GUANOSINE-5'-DIPHOSPHATE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (15 entities in total)
• Functional Keywords: tubulin, cytoskeleton, gtpase, transitional state, cell cycle
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 6
• Total formula weight: 267326.54

Authors

Oliva, M.A.,Estevez-Gallego, J.,Diaz, J.F.,Prota, A.E.,Steinmetz, M.O.,Balaguer, F.A.,Lucena-Agell, D. (deposition date: 2019-07-12, release date: 2020-02-19, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.25 Å)