biostudies-literatureDornes ADeutsche Forschungsgemeinschaft53-58https://www.ebi.ac.uk/biostudies/studies/S-EPMC10910532biostudies-literatureUnknown80(Pt 3)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.Acta crystallographica. Section F, Structural biology communicationsStructure of the GDP-bound state of the SRP GTPase FlhF.PMC10910532495924434Bange GDornes AMais CNfalseStructure of the GDP-bound state of the SRP GTPase FlhF.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.2024-01-01T00:00:00Z2024 Mar2026-06-16T04:54:07.618Z2025-04-06T17:16:59.324ZS-EPMC109105323837682310.1107/S2053230X24000979