5KH0

Crystal Structure of HydF from thermosipho melanesiensis in complex with a [4Fe-4S] cluster

Summary for 5KH0

• Entry DOI: 10.2210/pdb5kh0/pdb
• Descriptor: Small GTP-binding protein, IRON/SULFUR CLUSTER (2 entities in total)
• Functional Keywords: [fefe]-hydrogenase maturase oxidoreductase, oxidoreductase
• Biological source: Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429)
• Total number of polymer chains: 4
• Total formula weight: 178826.03

Authors

Caserta, G.,Pecqueur, L.,Fontecave, M. (deposition date: 2016-06-14, release date: 2017-05-03, Last modification date: 2024-05-08)

Primary citation

Caserta, G.,Pecqueur, L.,Adamska-Venkatesh, A.,Papini, C.,Roy, S.,Artero, V.,Atta, M.,Reijerse, E.,Lubitz, W.,Fontecave, M.
Structural and functional characterization of the hydrogenase-maturation HydF protein.
Nat. Chem. Biol., 13:779-784, 2017

PubMed Abstract: [FeFe] hydrogenase (HydA) catalyzes interconversion between 2H and H at an active site composed of a [4Fe-4S] cluster linked to a 2Fe subcluster that harbors CO, CN and azapropanedithiolate (adt) ligands. HydE, HydG and HydF are the maturases specifically involved in the biosynthesis of the 2Fe subcluster. Using ligands synthesized by HydE and HydG, HydF assembles a di-iron precursor of the 2Fe subcluster and transfers it to HydA for maturation. Here we report the first X-ray structure of HydF with its [4Fe-4S] cluster. The cluster is chelated by three cysteines and an exchangeable glutamate, which allows the binding of synthetic mimics of the 2Fe subcluster. [Fe(adt)(CO)(CN)] is proposed to be the true di-iron precursor because, when bound to HydF, it matures HydA and displays features in Fourier transform infrared (FTIR) spectra that are similar to those of the native HydF active intermediate. A new route toward the generation of artificial hydrogenases, as combinations of HydF and such biomimetic complexes, is proposed on the basis of the observed hydrogenase activity of chemically modified HydF.

PubMed: 28553946
DOI: 10.1038/nchembio.2385

Experimental method

X-RAY DIFFRACTION (2.8 Å)