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Nature Structural Biology  5, 451 - 458 (1998)
doi:10.1038/nsb0698-451

Tubulin and FtsZ form a distinct family of GTPases

Eva Nogales1, 3, Kenneth H. Downing1, Linda A. Amos2 & Jan Löwe2

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

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

  3email: enogales@lbl.gov

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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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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