8QML

(2R,4R)-MeTDA bound HydE structure (control experiment)

Summary for 8QML

• Entry DOI: 10.2210/pdb8qml/pdb
• Related: 8QMK
• Descriptor: [FeFe] hydrogenase maturase subunit HydE, S-ADENOSYL-L-HOMOCYSTEINE, (2R,4R)-2-methyl-1,3-thiazolidine-2,4-dicarboxylic acid, ... (8 entities in total)
• Functional Keywords: [fefe]-hydrogenase, radical sam enzyme, hyde, maturase, complex-b, h-cluster, metal binding protein
• Biological source: Thermotoga maritima MSB8
• Total number of polymer chains: 1
• Total formula weight: 45158.54

Authors

Omeiri, J.,Martin, L.,Usclat, A.,Cherrier, M.V.,Nicolet, Y. (deposition date: 2023-09-22, release date: 2023-11-22, Last modification date: 2023-12-27)

Primary citation

Omeiri, J.,Martin, L.,Usclat, A.,Cherrier, M.V.,Nicolet, Y.
Maturation of the [FeFe]-Hydrogenase: Direct Transfer of the ( kappa 3 -cysteinate)Fe II (CN)(CO) 2 Complex B from HydG to HydE.
Angew.Chem.Int.Ed.Engl., 62:e202314819-e202314819, 2023

PubMed Abstract: [FeFe]-hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen. Their prowess stems from the intricate H-cluster, combining a [Fe S ] center with a binuclear iron center ([2Fe] ). In the latter, each iron atom is coordinated by a CO and CN ligand, connected by a CO and an azadithiolate ligand. The synthesis of this active site involves a unique multiprotein assembly, featuring radical SAM proteins HydG and HydE. HydG initiates the transformation of L-tyrosine into cyanide and carbon monoxide to generate complex B, which is subsequently transferred to HydE to continue the biosynthesis of the [2Fe] -subcluster. Due to its instability, complex B isolation for structural or spectroscopic characterization has been elusive thus far. Nevertheless, the use of a biomimetic analogue of complex B allowed circumvention of the need for the HydG protein during in vitro functional investigations, implying a similar structure for complex B. Herein, we used the HydE protein as a nanocage to encapsulate and stabilize the complex B product generated by HydG. Using X-ray crystallography, we successfully determined its structure at 1.3 Å resolution. Furthermore, we demonstrated that complex B is directly transferred from HydG to HydE, thus not being released into the solution post-synthesis, highlighting a transient interaction between the two proteins.

PubMed: 37962296
DOI: 10.1002/anie.202314819

Experimental method

X-RAY DIFFRACTION (1.4 Å)