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TitleStructure and functionality of a multimeric human COQ7:COQ9 complex.
Journal, issue, pagesMol Cell, Vol. 82, Issue 22, Page 4307-4323.e10, Year 2022
Publish dateNov 17, 2022
AuthorsMateusz Manicki / Halil Aydin / Luciano A Abriata / Katherine A Overmyer / Rachel M Guerra / Joshua J Coon / Matteo Dal Peraro / Adam Frost / David J Pagliarini /
PubMed AbstractCoenzyme Q (CoQ) is a redox-active lipid essential for core metabolic pathways and antioxidant defense. CoQ is synthesized upon the mitochondrial inner membrane by an ill-defined "complex Q" ...Coenzyme Q (CoQ) is a redox-active lipid essential for core metabolic pathways and antioxidant defense. CoQ is synthesized upon the mitochondrial inner membrane by an ill-defined "complex Q" metabolon. Here, we present structure-function analyses of a lipid-, substrate-, and NADH-bound complex comprising two complex Q subunits: the hydroxylase COQ7 and the lipid-binding protein COQ9. We reveal that COQ7 adopts a ferritin-like fold with a hydrophobic channel whose substrate-binding capacity is enhanced by COQ9. Using molecular dynamics, we further show that two COQ7:COQ9 heterodimers form a curved tetramer that deforms the membrane, potentially opening a pathway for the CoQ intermediates to translocate from the bilayer to the proteins' lipid-binding sites. Two such tetramers assemble into a soluble octamer with a pseudo-bilayer of lipids captured within. Together, these observations indicate that COQ7 and COQ9 cooperate to access hydrophobic precursors within the membrane and coordinate subsequent synthesis steps toward producing CoQ.
External linksMol Cell / PubMed:36306796 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.5 Å
Structure data

25412

7ssp

EMDB-25412, PDB-7ssp:
Structure of the human COQ7:COQ9 complex by single-particle electron cryo-microscopy, unliganded state
Method: EM (single particle) / Resolution: 3.5 Å

25413

7sss

EMDB-25413, PDB-7sss:
Structure of the NADH-bound human COQ7:COQ9 complex by single-particle electron cryo-microscopy
Method: EM (single particle) / Resolution: 2.4 Å

Chemicals

ChemComp-PEV:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / POPE, phospholipid*YM / Phosphatidylethanolamine

ChemComp-8PP:
2-[(2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-OCTAMETHYLDOTRIACONTA-2,6,10,14,18,22,26,30-OCTAENYL]PHENOL

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / hydroxylase / complex / lipid / enzyme / NADH / coenzymeQ / isoprene / OPP

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