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Tubulin and FtsZ form a distinct family of GTPases

Nature Structural Biology volume 5, pages 451–458 (1998)Cite this article

Abstract

Tubulin and FtsZ share a common fold of two domains connected by a central helix. Structure-based sequence alignment shows that common residues localize in the nucleotide-binding site and a region that interacts with the nucleotide of the next tubulin subunit in the protofilament, suggesting that tubulin and FtsZ use similar contacts to form filaments. Surfaces that would make lateral interactions between protofilaments or interact with motor proteins are, however, different. The highly conserved nucleotide-binding sites of tubulin and FtsZ clearly differ from those of EF-Tu and other GTPases, while resembling the nucleotide site of glyceraldehyde-3-phosphate dehydrogenase. Thus, tubulin and FtsZ form a distinct family of GTP-hydrolyzing proteins.

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Author information

Authors and Affiliations

  1. Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Donner Laboratory, Berkeley, California, 94720, USA

    Eva Nogales & Kenneth H. Downing

  2. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Linda A. Amos & Jan Löwe

Authors
  1. Eva Nogales
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  2. Kenneth H. Downing
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  3. Linda A. Amos
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  4. Jan Löwe
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Correspondence to Eva Nogales.

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Nogales, E., Downing, K., Amos, L. et al. Tubulin and FtsZ form a distinct family of GTPases. Nat Struct Mol Biol 5, 451–458 (1998). https://doi.org/10.1038/nsb0698-451

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