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Tubulin and FtsZ form a distinct family of GTPases

Nature Structural Biology volume 5, pages 451458 (1998) | Download Citation

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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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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

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Correspondence to Eva Nogales.

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DOI

https://doi.org/10.1038/nsb0698-451

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