4.7 Article

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

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 412, Issue 1, Pages 35-42

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.07.029

Keywords

cytoskeleton; microtubule dynamics; nucleotide; tubulin structural cycle; X-ray crystallography

Funding

  1. Agence Nationale de la Recherche [ANR-09-BLAN-0071]
  2. Centre National de la Recherche Scientifique
  3. Fondation pour la Recherche Medicale [DEQ20081213979]
  4. Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0071] Funding Source: Agence Nationale de la Recherche (ANR)

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Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to alpha beta-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. (C) 2011 Elsevier Ltd. All rights reserved.

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