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Structure paper

TitleMolecular mechanism of the ischemia-induced regulatory switch in mammalian complex I.
Journal, issue, pagesScience, Vol. 384, Issue 6701, Page 1247-1253, Year 2024
Publish dateJun 14, 2024
AuthorsDaniel N Grba / John J Wright / Zhan Yin / William Fisher / Judy Hirst /
PubMed AbstractRespiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and ...Respiratory complex I is an efficient driver for oxidative phosphorylation in mammalian mitochondria, but its uncontrolled catalysis under challenging conditions leads to oxidative stress and cellular damage. Ischemic conditions switch complex I from rapid, reversible catalysis into a dormant state that protects upon reoxygenation, but the molecular basis for the switch is unknown. We combined precise biochemical definition of complex I catalysis with high-resolution cryo-electron microscopy structures in the phospholipid bilayer of coupled vesicles to reveal the mechanism of the transition into the dormant state, modulated by membrane interactions. By implementing a versatile membrane system to unite structure and function, attributing catalytic and regulatory properties to specific structural states, we define how a conformational switch in complex I controls its physiological roles.
External linksScience / PubMed:38870289
MethodsEM (single particle)
Resolution2.5 - 3.8 Å
Structure data

EMDB-18051, PDB-8q0a:
Inward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-18052, PDB-8q0f:
Inward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-18054: Inward-facing, slack proteoliposome complex I at 3.1 A. Initially purified in DDM.
PDB-8q0j: Inward-facing, slack proteoliposome complex I at 3.8 A. Initially purified in DDM.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-18055, PDB-8q0m:
Outward-facing, closed proteoliposome complex I at 3.1 A. Initially purified in DDM.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-18057, PDB-8q0o:
Outward-facing, open2 proteoliposome complex I at 3.1 A. Initially purified in DDM.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-18059: Outward-facing, slack proteoliposome complex I at 3.1 A. Initially purified in DDM.
PDB-8q0q: Outward-facing, slack proteoliposome complex I at 3.6 A. Initially purified in DDM
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-18066, PDB-8q1p:
Inward-facing, open2 proteoliposome complex I at 2.9 A, after deactivation treatment. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-18067, PDB-8q1u:
Inward-facing, open1 proteoliposome complex I at 3.3 A, after deactivation treatment. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-18068, PDB-8q1y:
Outward-facing, open2 proteoliposome complex I at 2.6 A, after deactivation treatment. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-18069, PDB-8q25:
Outward-facing, open1 proteoliposome complex I at 2.8 A, after deactivation treatment. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-18138, PDB-8q45:
Inward-facing, closed proteoliposome complex I at 2.7 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-18139, PDB-8q46:
Inward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-18140, PDB-8q47:
Inward-facing, open1 proteoliposome complex I at 2.9 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-18141, PDB-8q48:
Outward-facing, closed proteoliposome complex I at 2.5 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-18142, PDB-8q49:
Outward-facing, open2 proteoliposome complex I at 2.6 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-18143, PDB-8q4a:
Outward-facing, open1 proteoliposome complex I at 2.6 A. Initially purified in LMNG.
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

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

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-K:
Unknown entry

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-DGT:
2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-EHZ:
~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate

ChemComp-CHD:
CHOLIC ACID

ChemComp-MYR:
MYRISTIC ACID

ChemComp-U10:
UBIQUINONE-10

ChemComp-HOH:
WATER

ChemComp-FVH:
[[(2~{R},3~{S},4~{R},5~{R})-5-[(3~{R})-3-aminocarbonylpiperidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{R},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate

Source
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / Complex I / Oxidoreductase / Proteoliposomes / Membrane-bound / metabolism

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