6TTL

crystal structure of [FeFe]-hydrogenase CbA5H (partial) from Clostridium beijerinckii in Hinact state

Summary for 6TTL

• Entry DOI: 10.2210/pdb6ttl/pdb
• Related: 4XDC
• Descriptor: [FeFe]-hydrogenase, dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+), IRON/SULFUR CLUSTER (3 entities in total)
• Functional Keywords: [fefe]-hydrogenase, aerobically crystallized, clostridium beijerinckii, oxidoreductase
• Biological source: Clostridium beijerinckii
• Total number of polymer chains: 2
• Total formula weight: 151417.06

Authors

Duan, J.,Rutz, A.,Hofmann, E.,Happe, T. (deposition date: 2019-12-28, release date: 2020-12-09, Last modification date: 2024-01-24)

Primary citation

Winkler, M.,Duan, J.,Rutz, A.,Felbek, C.,Scholtysek, L.,Lampret, O.,Jaenecke, J.,Apfel, U.P.,Gilardi, G.,Valetti, F.,Fourmond, V.,Hofmann, E.,Leger, C.,Happe, T.
A safety cap protects hydrogenase from oxygen attack.
Nat Commun, 12:756-756, 2021

PubMed Abstract: [FeFe]-hydrogenases are efficient H-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-transform infrared spectroscopy to describe a protein morphing mechanism that controls the reversible transition between the catalytic H-state and the inactive but oxygen-resistant H-state in [FeFe]-hydrogenase CbA5H of Clostridium beijerinckii. The X-ray structure of air-exposed CbA5H reveals that a conserved cysteine residue in the local environment of the active site (H-cluster) directly coordinates the substrate-binding site, providing a safety cap that prevents O-binding and consequently, cofactor degradation. This protection mechanism depends on three non-conserved amino acids situated approximately 13 Å away from the H-cluster, demonstrating that the 1st coordination sphere chemistry of the H-cluster can be remote-controlled by distant residues.

PubMed: 33531463
DOI: 10.1038/s41467-020-20861-2

Experimental method

X-RAY DIFFRACTION (2.9 Å)