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TitleLong-range charge transfer mechanism of the IIIIV mycobacterial supercomplex.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5276, Year 2024
Publish dateJun 20, 2024
AuthorsDaniel Riepl / Ana P Gamiz-Hernandez / Terezia Kovalova / Sylwia M Król / Sophie L Mader / Dan Sjöstrand / Martin Högbom / Peter Brzezinski / Ville R I Kaila /
PubMed AbstractAerobic life is powered by membrane-bound redox enzymes that shuttle electrons to oxygen and transfer protons across a biological membrane. Structural studies suggest that these energy-transducing ...Aerobic life is powered by membrane-bound redox enzymes that shuttle electrons to oxygen and transfer protons across a biological membrane. Structural studies suggest that these energy-transducing enzymes operate as higher-order supercomplexes, but their functional role remains poorly understood and highly debated. Here we resolve the functional dynamics of the 0.7 MDa IIIIV obligate supercomplex from Mycobacterium smegmatis, a close relative of M. tuberculosis, the causative agent of tuberculosis. By combining computational, biochemical, and high-resolution (2.3 Å) cryo-electron microscopy experiments, we show how the mycobacterial supercomplex catalyses long-range charge transport from its menaquinol oxidation site to the binuclear active site for oxygen reduction. Our data reveal proton and electron pathways responsible for the charge transfer reactions, mechanistic principles of the quinone catalysis, and how unique molecular adaptations, water molecules, and lipid interactions enable the proton-coupled electron transfer (PCET) reactions. Our combined findings provide a mechanistic blueprint of mycobacterial supercomplexes and a basis for developing drugs against pathogenic bacteria.
External linksNat Commun / PubMed:38902248 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 2.8 Å
Structure data

17210

8ovc

EMDB-17210, PDB-8ovc:
Respiratory supercomplex (III2-IV2) from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 2.8 Å

17211

8ovd

EMDB-17211, PDB-8ovd:
Respiratory supercomplex (III2-IV2) from Mycobacterium smegmatis
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

ChemComp-HEC:
HEME C

ChemComp-MQ9:
MENAQUINONE-9


ChemComp, No image

ChemComp-WUO:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-9YF:
(2R)-2-(hexadecanoyloxy)-3-{[(S)-hydroxy{[(1R,2R,3R,4R,5R,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propyl (9S)-9-methyloctadecanoate

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-7PH:
(1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate

ChemComp-HEA:
HEME-A

ChemComp-CU:
COPPER (II) ION

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-9XX:
(2S)-1-(hexadecanoyloxy)propan-2-yl (10S)-10-methyloctadecanoate

ChemComp-PLM:
PALMITIC ACID

ChemComp-HOH:
WATER

ChemComp-IZL:
[(2~{R})-3-[[(1~{S},2~{R},3~{S},4~{S},5~{R},6~{R})-2-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-[[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,5-bis(oxidanyl)oxan-2-yl]oxymethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxymethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,4,5-tris(oxidanyl)-6-[(2~{R},3~{S},4~{S},5~{S},6~{R})-3,4,5-tris(oxidanyl)-6-(undecanoyloxymethyl)oxan-2-yl]oxy-cyclohexyl]oxy-oxidanyl-phosphoryl]oxy-2-undecanoyloxy-propyl] (10~{R})-10-methyldodecanoate

ChemComp-TRD:
TRIDECANE

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

Source
  • mycolicibacterium smegmatis (bacteria)
KeywordsELECTRON TRANSPORT / RESPIRATORY SUPERCOMPLEX / MEMBRANE PROTEIN / ACTINOBACTERIA

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