Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular mechanism of the ischemia-induced regulatory switch in mammalian complex I.
Journal, issue, pages	Science, Vol. 384, Issue 6701, Page 1247-1253, Year 2024
Publish date	Jun 14, 2024
Authors	Daniel N Grba / John J Wright / Zhan Yin / William Fisher / Judy Hirst /
PubMed Abstract	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 ...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 links	Science / PubMed:38870289
Methods	EM (single particle)
Resolution	2.5 - 3.8 Å
Structure data	18051 8q0a 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 18052 8q0f 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 18054 8q0j 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 18055 8q0m 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 18057 8q0o 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 18059 8q0q 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 18066 8q1p 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 18067 8q1u 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 18068 8q1y 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 18069 8q25 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 18138 8q45 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 18139 8q46 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 18140 8q47 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 18141 8q48 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 18142 8q49 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 18143 8q4a 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 / phospholipidYM ChemComp-PC1: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM ChemComp-PLC: DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipidYM ChemComp-SF4: IRON/SULFUR CLUSTER ChemComp-FES: FE2/S2 (INORGANIC) CLUSTER ChemComp-FMN: FLAVIN MONONUCLEOTIDE ChemComp-K: Unknown entry ChemComp-CDL: CARDIOLIPIN / phospholipidYM 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)
Keywords	MEMBRANE PROTEIN / Complex I / Oxidoreductase / Proteoliposomes / Membrane-bound / metabolism