{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dornes A"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["53-58"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10910532"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["80(Pt 3)"],"pubmed_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."],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Structure of the GDP-bound state of the SRP GTPase FlhF."],"pmcid":["PMC10910532"],"funding_grant_id":["495924434"],"pubmed_authors":["Bange G","Dornes A","Mais CN"],"additional_accession":[]},"is_claimable":false,"name":"Structure of the GDP-bound state of the SRP GTPase FlhF.","description":"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.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-16T04:54:07.618Z","creation":"2025-04-06T17:16:59.324Z"},"accession":"S-EPMC10910532","cross_references":{"pubmed":["38376823"],"doi":["10.1107/S2053230X24000979"]}}