Fig. 7From: Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and functionFtsZ84*M206I and FtsZ84*V293I mutations compensate FtsZ84 to increase GTPase activity and longitudinal subunit interactions. a Wild-type FtsZ efficiently binds to and hydrolyzes GTP (black rectangle). This promotes subunit interactions and polymerization. b FtsZ84 contains a mutation in the GTP binding site that reduces GTP binding and hydrolysis, thereby weakening FtsZ dimerization and subunit-subunit assembly. c FtsZ84*M206I and FtsZ84*V293I mutations compensate for FtsZ84’s GTP binding defect and help to restore subunit-subunit interactions. d Introducing FtsZ84*M206I and FtsZ84*V293I into wild-type FtsZ reduces GTPase activity and assemblyBack to article page