%0 Journal Article
%T Structure of the GDP-bound state of the SRP GTPase FlhF.
%A Dornes A
%A Mais CN
%A Bange G
%J Acta Crystallogr F Struct Biol Commun
%V 80
%N 0
%D 2024 Mar 1
%M 38376823
%F 1.072
%R 10.1107/S2053230X24000979
%X The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.