NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex.

ABSTRACT: The Min system is a key spatial regulator of cell division in rod-shaped bacteria and the first FtsZ-negative modulator to be recognized. Nevertheless, despite extensive genetic and in vitro studies, the molecular mechanism used by MinC to inhibit Z-ring formation remains incompletely understood. The crystallization of FtsZ in complex with other negative regulators such as SulA and MciZ has provided important structural information to corroborate in vitro experiments and establish the mechanism of Z-ring antagonism by these modulators. However, MinC and FtsZ have so far eluded co-crystallization, probably because their complex is too unstable to be crystallized. To gain structural insight into the mechanism of action of MinC, we determined the solution structure of the N-terminal domain of

SUBMITTER: Machado LESF 

PROVIDER: S-EPMC11938149 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature