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Structure of the αβ tubulin dimer by electron crystallography

Author

Listed:
  • Eva Nogales

    (Lawrence Berkeley National Laboratory)

  • Sharon G. Wolf

    (Weizmann Institute of Science)

  • Kenneth H. Downing

    (Lawrence Berkeley National Laboratory)

Abstract

The αβ tubulin heterodimer is the structural subunit of microtubules, which are cytoskeletal elements that are essential for intracellular transport and cell division in all eukaryotes. Each tubulin monomer binds a guanine nucleotide, which is non-exchangeable when it is bound in the α subunit, or N site, and exchangeable when bound in the β subunit, or E site. The α- and β-tubulins share 40% amino-acid sequence identity, both exist in several isotype forms, and both undergo a variety of post-translational modifications1. Limited sequence homology has been found with the proteins FtsZ2 and Misato3, which are involved in cell division in bacteria and Drosophila, respectively. Here we present an atomic model of the αβ tubulin dimer fitted to a 3.7-Å density map obtained by electron crystallography of zinc-induced tubulin sheets. The structures of α- and β-tubulin are basically identical: each monomer is formed by a core of two β-sheets surrounded by α-helices. The monomer structure is very compact, but can be divided into three functional domains: the amino-terminal domain containing the nucleotide-binding region, an intermediate domain containing the Taxol-binding site, and the carboxy-terminal domain, which probably constitutes the binding surface for motor proteins.

Suggested Citation

  • Eva Nogales & Sharon G. Wolf & Kenneth H. Downing, 1998. "Structure of the αβ tubulin dimer by electron crystallography," Nature, Nature, vol. 391(6663), pages 199-203, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6663:d:10.1038_34465
    DOI: 10.1038/34465
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    Cited by:

    1. Ishutesh Jain & Mandar M Inamdar & Ranjith Padinhateeri, 2015. "Statistical Mechanics Provides Novel Insights into Microtubule Stability and Mechanism of Shrinkage," PLOS Computational Biology, Public Library of Science, vol. 11(2), pages 1-23, February.
    2. Shirmovsky, S.Eh. & Shulga, D.V., 2023. "Quantum relaxation processes in microtubule tryptophan system," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 617(C).
    3. Chen, Ying & Qiu, Xi-Jun & Dong, Xian-Lin, 2006. "A theory for cell microtubule wall in external field and pseudo-spin wave excitation," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 365(2), pages 463-472.

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