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    Nat Struct Biol. 1998 Jun;5(6):451-8.

    Tubulin and FtsZ form a distinct family of GTPases.

    Nogales E, Downing KH, Amos LA, Löwe J.

    Source

    Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. enogales@lbl.gov

    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.

    PMID:
    9628483
    [PubMed - indexed for MEDLINE]

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