8qml | pdb_00008qml

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

spinqualitylabelsall models 8qml, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qml is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: 41K, CL, CPS, OTY, SAH, SF4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HYDE_THEMA Required for the maturation of the [FeFe]-hydrogenase HydA (By similarity). Catalyzes the reductive cleavage of S-adenosyl-L-methionine (in vitro), suggesting it may contribute to the biosynthesis of an essential sulfur-containing ligand that binds to the hydrogenase active site [2Fe-2S] cluster (PubMed:16137685).[UniProtKB:Q97IK9] Publication Abstract from PubMed FeFe]-hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen. Their prowess stems from the intricate H-cluster, combining a [Fe4S4] center with a binuclear iron center ([2Fe]H). 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]H-subcluster. Due to its instability, complex-B isolation for structural or spectroscopic characterization has been elusive this far. Nevertheless, the use of a biomimetic compound of complex-B allowed circumventing the need for the HydG protein during in vitro functional investigations, implying a similar structure for complex-B. Here, 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 A 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. Maturation of the [FeFe]-Hydrogenase: Direct Transfer of the (kappa3-cysteinate)FeII(CN)(CO)2 Complex-B from HydG to HydE.,Omeiri J, Martin L, Usclat A, Cherrier MV, Nicolet Y Angew Chem Int Ed Engl. 2023 Nov 14:e202314819. doi: 10.1002/anie.202314819. PMID:37962296 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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