{Reference Type}: Journal Article
{Title}: Structure of the GDP-bound state of the SRP GTPase FlhF.
{Author}: Dornes A;Mais CN;Bange G;
{Journal}: Acta Crystallogr F Struct Biol Commun
{Volume}: 80
{Issue}: 0
{Year}: 2024 Mar 1
{Factor}: 1.072
{DOI}: 10.1107/S2053230X24000979
{Abstract}: 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.