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J Mol Biol. 2011 Sep 9;412(1):35-42. doi: 10.1016/j.jmb.2011.07.029. Epub 2011 Jul 23.

The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin.

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Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), Centre de Recherche de Gif, CNRS, Bat. 34, 1, avenue de la Terrasse, 91198 Gif sur Yvette, France.


Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to αβ-tubulin is required for microtubule assembly, but whether this triggers conversion into a straighter structure is still debated. This is due, at least in part, to the lack of structural data for GTP-tubulin before assembly. Here, we report atomic-resolution crystal structures of soluble tubulin in the GDP and GTP nucleotide states in a complex with a stathmin-like domain. The structures differ locally in the neighborhood of the nucleotide. A loop movement in GTP-bound tubulin favors its recruitment to the ends of growing microtubules and facilitates its curved-to-straight transition, but this conversion has not proceeded yet. The data therefore argue for the conformational change toward the straight structure occurring as microtubule-specific contacts are established. They also suggest a model for the way the tubulin structure is modified in relation to microtubule assembly.

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