Download MendeleyStructural Insights Into Ftsz Protofilament Formation
Oliva, M.A., Cordell, S.C., Lowe, J.(2004) Nat Struct Mol Biol 11: 1243
- PubMed: 15558053
- DOI: https://doi.org/10.1038/nsmb855
- Primary Citation of Related Structures:
1W58, 1W59, 1W5A, 1W5B, 1W5E, 1W5F - PubMed Abstract:
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.
Organizational Affiliation:
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
