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Structural insights into FtsZ protofilament formation.
Maria A Oliva1, Suzanne C Cordell, Jan Löwe
1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Nature Structural & Molecular Biology
|November 24, 2004
Summary
Bacterial cell division protein FtsZ polymerizes into filaments. Structural analysis reveals how its N- and C-terminal domains form the GTPase site, offering insights into FtsZ and tubulin evolution and polymerization dynamics.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- The prokaryotic tubulin homolog FtsZ is crucial for bacterial cell division, polymerizing into filaments.
- Understanding FtsZ structure and function is key to bacterial cell biology and potential antimicrobial targets.
Purpose of the Study:
- To elucidate the structural basis of FtsZ polymerization and GTPase activity.
- To model the evolutionary relationship between FtsZ and eukaryotic tubulin.
Main Methods:
- Crystallization of refolded FtsZ into a tubulin-like protofilament.
- Determination of crystal structures of FtsZ in different nucleotide states.
- Biochemical analysis of purified FtsZ N- and C-terminal domains.
Main Results:
- The N- and C-terminal domains of FtsZ subunits form the GTPase site within the filament.
- FtsZ domains are structurally independent, suggesting an evolutionary fusion model with tubulin.
- The nucleotide-binding pocket in FtsZ filaments allows nucleotide exchange, making hydrolysis rate-limiting, unlike occluded tubulin.
Conclusions:
- FtsZ polymerization dynamics differ from tubulin due to nucleotide accessibility.
- The study proposes a model for the evolution of tubulin polymerization from ancestral two-domain proteins like FtsZ.
- Structural similarities and differences between FtsZ and tubulin provide insights into cytoskeletal evolution.