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Open data
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Basic information
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Title | Deactive state CI from Q10-NADH dataset, Subclass 1 | ||||||||||||
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![]() | mammalian / mitochondrial / respiratory / complex I / ELECTRON TRANSPORT | ||||||||||||
Function / homology | ![]() Mitochondrial protein import / RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Neutrophil degranulation / : / Mitochondrial protein degradation / cardiac muscle tissue development / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) ...Mitochondrial protein import / RHOG GTPase cycle / Complex I biogenesis / Respiratory electron transport / Neutrophil degranulation / : / Mitochondrial protein degradation / cardiac muscle tissue development / oxidoreductase activity, acting on NAD(P)H / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / reactive oxygen species metabolic process / aerobic respiration / respiratory electron transport chain / electron transport chain / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / fatty acid biosynthetic process / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / nuclear body / nuclear speck / mitochondrial matrix / mitochondrion / nucleoplasm / membrane / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||
![]() | Gu JK / Yang MJ | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The coupling mechanism of mammalian mitochondrial complex I. Authors: Jinke Gu / Tianya Liu / Runyu Guo / Laixing Zhang / Maojun Yang / ![]() Abstract: Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in ...Mammalian respiratory complex I (CI) is a 45-subunit, redox-driven proton pump that generates an electrochemical gradient across the mitochondrial inner membrane to power ATP synthesis in mitochondria. In the present study, we report cryo-electron microscopy structures of CI from Sus scrofa in six treatment conditions at a resolution of 2.4-3.5 Å, in which CI structures of each condition can be classified into two biochemical classes (active or deactive), with a notably higher proportion of active CI particles. These structures illuminate how hydrophobic ubiquinone-10 (Q10) with its long isoprenoid tail is bound and reduced in a narrow Q chamber comprising four different Q10-binding sites. Structural comparisons of active CI structures from our decylubiquinone-NADH and rotenone-NADH datasets reveal that Q10 reduction at site 1 is not coupled to proton pumping in the membrane arm, which might instead be coupled to Q10 oxidation at site 2. Our data overturn the widely accepted previous proposal about the coupling mechanism of CI. | ||||||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 14.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 54.9 KB 54.9 KB | Display Display | ![]() |
Images | ![]() | 81.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 437.6 KB | Display | ![]() |
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Full document | ![]() | 437.2 KB | Display | |
Data in XML | ![]() | 6.2 KB | Display | |
Data in CIF | ![]() | 7.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7w1oMC ![]() 7v2cC ![]() 7v2dC ![]() 7v2eC ![]() 7v2fC ![]() 7v2hC ![]() 7v2kC ![]() 7v2rC ![]() 7v30C ![]() 7v31C ![]() 7v32C ![]() 7v33C ![]() 7v3mC ![]() 7vb7C ![]() 7vblC ![]() 7vbnC ![]() 7vbpC ![]() 7vbzC ![]() 7vc0C ![]() 7vwjC ![]() 7vwlC ![]() 7vxpC ![]() 7vxsC ![]() 7vxuC ![]() 7vy1C ![]() 7vy8C ![]() 7vy9C ![]() 7vyaC ![]() 7vyeC ![]() 7vyfC ![]() 7vygC ![]() 7vyhC ![]() 7vyiC ![]() 7vynC ![]() 7vysC ![]() 7vz1C ![]() 7vz8C ![]() 7vzvC ![]() 7vzwC ![]() 7w00C ![]() 7w0hC ![]() 7w0rC ![]() 7w0yC ![]() 7w1pC ![]() 7w1tC ![]() 7w1uC ![]() 7w1vC ![]() 7w1zC ![]() 7w20C ![]() 7w2kC ![]() 7w2lC ![]() 7w2rC ![]() 7w2uC ![]() 7w2yC ![]() 7w31C ![]() 7w32C ![]() 7w35C ![]() 7w4cC ![]() 7w4dC ![]() 7w4eC ![]() 7w4fC ![]() 7w4gC ![]() 7w4jC ![]() 7w4kC ![]() 7w4lC ![]() 7w4mC ![]() 7w4nC ![]() 7w4qC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0742 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Respiratory complex I
+Supramolecule #1: Respiratory complex I
+Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
+Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
+Macromolecule #4: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #5: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #6: Acyl carrier protein
+Macromolecule #7: Complex I subunit B13
+Macromolecule #8: Complex I-B14.5a
+Macromolecule #9: NADH dehydrogenase ubiquinone 1 alpha subcomplex subunit 9, mitoc...
+Macromolecule #10: Complex I-9kD
+Macromolecule #11: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #12: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
+Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #14: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #15: Complex I-30kD
+Macromolecule #16: Complex I-49kD
+Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #18: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #21: Complex I-B16.6
+Macromolecule #22: Complex I-AGGG
+Macromolecule #23: Complex I-B12
+Macromolecule #24: Complex I-SGDH
+Macromolecule #25: Complex I-B17
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #29: Complex I-KFYI
+Macromolecule #30: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #31: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #32: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #33: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #34: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #35: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #36: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #40: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #41: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #44: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #45: IRON/SULFUR CLUSTER
+Macromolecule #46: FLAVIN MONONUCLEOTIDE
+Macromolecule #47: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
+Macromolecule #48: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
+Macromolecule #49: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #50: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #51: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #52: MAGNESIUM ION
+Macromolecule #53: ZINC ION
+Macromolecule #54: CARDIOLIPIN
+Macromolecule #55: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,...
+Macromolecule #56: Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer
+Macromolecule #57: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 24886 |
Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: RANDOM ASSIGNMENT |