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6G72

Mouse mitochondrial complex I in the deactive state

Summary for 6G72
Entry DOI10.2210/pdb6g72/pdb
Related6G2J
EMDB information4345 4356
DescriptorNADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (52 entities in total)
Functional Keywordscomplex i, mitochondria, proton pump, membrane protein, oxidoreductase
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains45
Total formula weight1052147.47
Authors
Agip, A.N.A.,Blaza, J.N.,Bridges, H.R.,Viscomi, C.,Rawson, S.,Muench, S.P.,Hirst, J. (deposition date: 2018-04-04, release date: 2018-06-06, Last modification date: 2024-05-29)
Primary citationAgip, A.A.,Blaza, J.N.,Bridges, H.R.,Viscomi, C.,Rawson, S.,Muench, S.P.,Hirst, J.
Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states.
Nat. Struct. Mol. Biol., 25:548-556, 2018
Cited by
PubMed Abstract: Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I.
PubMed: 29915388
DOI: 10.1038/s41594-018-0073-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

227344

数据于2024-11-13公开中

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