Atomic structures of tubulin and FtsZ.
The recently published atomic structures of tubulin and FtsZ are a research milestone. The N-terminal GTP-binding domains of tubulin and FtsZ are virtually identical in structure, as expected from the substantial sequence identity. Sequence identity is absent from the C-terminal domains, but they also have virtually identical structures. A surprising finding is that the N-terminal GTP-binding domain is structurally homologous to that of Ras and other G proteins, despite the completely different GTP-binding sequence motifs. This article discusses these findings and the molecular mechanisms that can now be addressed with the atomic structures.
Erickson
H P
HP
Dept of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. H.Erickson@cellbio.duke.edu
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D019204:GTP-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D014404:Tubulin / Q000737:chemistry*
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D014404:Tubulin; D019204:GTP-Binding Proteins