Structure of the GDP-bound state of the SRP GTPase FlhF.

Autor: Dornes A; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, University of Marburg, Karl-von-Frisch-Strasse 14, 35043 Marburg, Germany., Mais CN; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, University of Marburg, Karl-von-Frisch-Strasse 14, 35043 Marburg, Germany., Bange G; Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, University of Marburg, Karl-von-Frisch-Strasse 14, 35043 Marburg, Germany.
Jazyk: angličtina
Zdroj: Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2024 Mar 01; Vol. 80 (Pt 3), pp. 53-58. Date of Electronic Publication: 2024 Feb 20.
DOI: 10.1107/S2053230X24000979
Abstrakt: 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.
(open access.)
Databáze: MEDLINE
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