Tubulin and FtsZ form a distinct family of GTPases

Nat Struct Biol. 1998 Jun;5(6):451-8. doi: 10.1038/nsb0698-451.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Cytoskeletal Proteins*
  • GTP Phosphohydrolases* / chemistry
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry
  • Guanosine Triphosphate / chemistry
  • Methanococcus
  • Models, Molecular
  • Molecular Sequence Data
  • NAD / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Swine
  • Tubulin / chemistry*


  • Bacterial Proteins
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Tubulin
  • NAD
  • Guanosine Triphosphate
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • GTP Phosphohydrolases

Associated data

  • PDB/1COM
  • PDB/1FSZ
  • PDB/1TUB