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.
Dept of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. H.Erickson@cellbio.duke.edu
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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