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Structural insights into FtsZ protofilament formation

Nature Structural & Molecular Biology volume 11, pages 1243–1250 (2004)Cite this article

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.

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Figure 1: FtsZ consists of two independent domains that can recombine noncovalently.
Figure 2: Crystal structure of a semicontinuous FtsZ protofilament.
Figure 3: Structure of the FtsZ dimer.
Figure 4: Detailed view of the intersubunit active sites in MjFtsZ and tubulin.
Figure 5: A lack of conformational changes in different FtsZ structures.

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Acknowledgements

We thank the Ministerio de Ciencia y Tecnologia, Spain for financial support to M.A. We also thank J.M. Andreu (Madrid) for supplying us with the MjFtsZ-W319Y plasmid. Finally, we had great support on the following beamlines: Synchtrotron Radiation Source (14.2 and 9.6) and European Synchrotron Radiation Facility (ID29 and BM14).

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  1. Maria A Oliva

    Present address: Centro de Investigaciones Biológicas (CIB-CSIC), c/ Ramiro de Maeztu, 9, 28040, Madrid, Spain

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Maria A Oliva, Suzanne C Cordell & Jan Löwe

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Correspondence to Jan Löwe.

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Oliva, M., Cordell, S. & Löwe, J. Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol 11, 1243–1250 (2004). https://doi.org/10.1038/nsmb855

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