Complex state transitions of the bacterial cell division protein FtsZ.

ABSTRACT: The key bacterial cell division protein FtsZ can adopt multiple conformations, and prevailing models suggest that transitions of FtsZ subunits from the closed to open state are necessary for filament formation and stability. Using all-atom molecular dynamics simulations, we analyzed state transitions of Staphylococcus aureus FtsZ as a monomer, dimer, and hexamer. We found that monomers can adopt intermediate states but preferentially adopt a closed state that is robust to forced reopening. Dimer subunits transitioned between open and closed states, and dimers with both subunits in the closed state remained highly stable, suggesting that open-state conformations are not necessary for filament formation. Mg²⁺ strongly stabilized the conformation of GTP-bound subunits and th

SUBMITTER: Knapp BD 

PROVIDER: S-EPMC11481701 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature