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Structure paper

TitleA scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 11, Page 2196-2202, Year 2025
Publish dateAug 25, 2025
AuthorsM Broc / M V Cherrier / A Uzel / R Arias-Cartin / P Arnoux / G Brasseur / F Seduk / B Guigliarelli / P Legrand / F Pierrel / G Schoehn / M J Maté / L Martin / S Grimaldi / Y Nicolet / A Magalon / A Walburger /
PubMed AbstractRedox 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 ...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.
External linksNat Struct Mol Biol / PubMed:40855134
MethodsEM (single particle) / X-ray diffraction
Resolution2.694 - 3.626 Å
Structure data

19452

8rr0

EMDB-19452, PDB-8rr0:
CryoEM structure of Molybdenum bispyranopterin guanine dinucleotide formate dehydrogenases ForCE1 from Bacillus subtilis
Method: EM (single particle) / Resolution: 3.35 Å

PDB-8rqz:
Crystal structure of Molybdenum bispyranopterin guanine dinucleotide formate dehydrogenases ForCE1 from Bacillus subtilis
Method: X-RAY DIFFRACTION / Resolution: 2.694 Å

PDB-9gzq:
Structure of ForCE lacking the Helical Membrane Plug-in (HMP; DUF1641)
Method: X-RAY DIFFRACTION / Resolution: 3.626 Å

Chemicals

ChemComp-MYR:
MYRISTIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-4MO:
MOLYBDENUM(IV) ION

ChemComp-MQ7:
MENAQUINONE-7

ChemComp-H2S:
HYDROSULFURIC ACID

ChemComp-MLI:
MALONATE ION

ChemComp-NO3:
NITRATE ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-11A:
UNDECANOIC ACID / antifungal*YM

PDB-1h2v:
Structure of the human nuclear cap-binding-complex (CBC)

ChemComp-SHV:
HEPTANOIC ACID

ChemComp-KNA:
nonanoic acid

Source
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
  • bacillus subtilis (bacteria)
KeywordsOXIDOREDUCTASE / Bacterial metabolism Bioenergetics Metalloenzyme Quinone Iron-Sulfur Cluster Helical Membrane Plug-in / ELECTRON TRANSPORT / Formate dehydrogenase / DUF1641

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