9gzq

Structure of ForCE lacking the Helical Membrane Plug-in (HMP; DUF1641)

spinqualitylabelsall models 9gzq, resolution 3.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9gzq is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.626Å Ligands: 4MO, FES, MGD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YJGC_BACSU Publication Abstract from PubMed Redox processes are at the heart of energetic metabolism that drives life on earth. By extension, complex and efficient electron transfer wires are necessary to connect the various metabolic pathways that are often located in distinct cellular compartments. Here, we uncovered a structural module that enables channeling of quinones from the membrane to various water-soluble redox catalytic units in prokaryotes. Using X-ray crystallography and cryo-electron microscopy, we determined the structure of the unusual bacterial formate dehydrogenase ForCE that contains four ForC catalytic subunits docked around a membrane-associated tetrameric ForE central scaffold. In the latter, a conserved domain that we propose to name helical membrane plugin (HMP) was identified as essential to link formate oxidation, in Bacillus subtilis, to the aerobic respiratory chain. Our bioinformatic analysis indicates that this HMP is associated with different quinone-reducing oxidoreductases, highlighting its broad importance as a functional unit to wire electrons between a given catalytic redox center and the quinone pool. A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.,Broc M, Cherrier MV, Uzel A, Arias-Cartin R, Arnoux P, Brasseur G, Seduk F, Guigliarelli B, Legrand P, Pierrel F, Schoehn G, Mate MJ, Martin L, Grimaldi S, Nicolet Y, Magalon A, Walburger A Nat Struct Mol Biol. 2025 Aug 25. doi: 10.1038/s41594-025-01607-4. PMID:40855134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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