Structural insights into FtsZ protofilament formation

Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. doi: 10.1038/nsmb855. Epub 2004 Nov 21.


The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / ultrastructure
  • Binding Sites
  • Circular Dichroism
  • Crystallography, X-Ray
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / ultrastructure
  • Dimerization
  • GTP Phosphohydrolases / metabolism
  • Methanococcus / chemistry
  • Methanococcus / metabolism
  • Microscopy, Electron
  • Models, Molecular
  • Mutation / genetics
  • Protein Structure, Tertiary
  • Thermotoga maritima / chemistry*
  • Thermotoga maritima / genetics
  • Tubulin / chemistry
  • Tubulin / metabolism
  • Water / chemistry


  • Bacterial Proteins
  • Cytoskeletal Proteins
  • FtsZ protein, Bacteria
  • Tubulin
  • Water
  • GTP Phosphohydrolases

Associated data

  • PDB/1W58
  • PDB/1W59
  • PDB/1W5A
  • PDB/1W5B
  • PDB/1W5E
  • PDB/1W5F