Crystal structure of the bacterial cell division inhibitor MinC

Bacterial cell division requires accurate selection of the middle of the ce ll, where the bacterial tubulin homologue FtsZ polymerizes into a ring stru cture. In Escherichia coli, site selection is dependent on MinC, MinD and M inE, MinC acts, with MinD, to inhibit division at sites other than the midc ell by directly interacting with FtsZ, Here we report the crystal structure to 2.2 Angstrom of MinC from Thermotoga maritima, MinC consists of two dom ains separated by a short linker. The C-terminal domain is a right-handed P -helix and is involved in dimer formation. The crystals contain two differe nt MinC dimers, demonstrating flexibility in the linker region. The two-dom ain architecture and dimerization of MinC can be rationalized with a model of cell division inhibition. MinC does not act like SulA, which affects the GTPase activity of FtsZ, and the model can explain how MinC would select f or the FtsZ polymer rather than the monomer.