Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch.

ABSTRACT: [FeFe]-hydrogenases catalyse the reduction of protons to hydrogen at a complex 2Fe[4Fe4S] center called H-cluster. The assembly of this active site is a multistep process involving three proteins, HydE, HydF and HydG. According to the current models, HydF has the key double role of scaffold, upon which the final H-cluster precursor is assembled, and carrier to transfer it to the target hydrogenase. The X-ray structure of HydF indicates that the protein is a homodimer with both monomers carrying two functional domains: a C-terminal FeS cluster-binding domain, where the precursor is assembled, and a N-terminal GTPase domain, whose exact contribution to cluster biogenesis and hydrogenase activation is still elusive. We previously obtained several hints suggesting that the binding of GTP to Hy

SUBMITTER: Galazzo L 

PROVIDER: S-EPMC5431965 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature