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The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin

Abstract : 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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https://hal.archives-ouvertes.fr/hal-02120600
Contributor : Benoît Gigant <>
Submitted on : Monday, May 6, 2019 - 8:36:11 AM
Last modification on : Thursday, November 19, 2020 - 8:50:29 AM

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Agata Nawrotek, Marcel Knossow, Benoît Gigant. The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin. Journal of Molecular Biology, Elsevier, 2011, 412 (1), pp.35-42. ⟨10.1016/j.jmb.2011.07.029⟩. ⟨hal-02120600⟩

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