+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11243 | |||||||||
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Title | Membrane domain of closed complex I during turnover | |||||||||
Map data | Oversampled, local resolution-filtered map | |||||||||
Sample |
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Function / homology | Function and homology information NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / : / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / : ...NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / : / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / : / ATP synthesis coupled electron transport / reactive oxygen species metabolic process / electron transport chain / mitochondrial intermembrane space / membrane => GO:0016020 / mitochondrial inner membrane / mitochondrial matrix Similarity search - Function | |||||||||
Biological species | Ovis aries (sheep) / Sheep (sheep) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Kampjut D / Sazanov LA | |||||||||
Funding support | European Union, 2 items
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Citation | Journal: Science / Year: 2020 Title: The coupling mechanism of mammalian respiratory complex I. Authors: Domen Kampjut / Leonid A Sazanov / Abstract: Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different ...Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during open-to-closed state transitions of the enzyme. In the induced deactive state, the open conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11243.map.gz | 149.8 MB | EMDB map data format | |
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Header (meta data) | emd-11243-v30.xml emd-11243.xml | 40.4 KB 40.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_11243_fsc.xml | 17.8 KB | Display | FSC data file |
Images | emd_11243.png | 192.1 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11243 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11243 | HTTPS FTP |
-Validation report
Summary document | emd_11243_validation.pdf.gz | 284.6 KB | Display | EMDB validaton report |
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Full document | emd_11243_full_validation.pdf.gz | 283.7 KB | Display | |
Data in XML | emd_11243_validation.xml.gz | 12.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11243 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11243 | HTTPS FTP |
-Related structure data
Related structure data | 6zkbMC 6zk9C 6zkaC 6zkcC 6zkdC 6zkeC 6zkfC 6zkgC 6zkhC 6zkiC 6zkjC 6zkkC 6zklC 6zkmC 6zknC 6zkoC 6zkpC 6zkqC 6zkrC 6zksC 6zktC 6zkuC 6zkvC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_11243.map.gz / Format: CCP4 / Size: 163.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Oversampled, local resolution-filtered map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : Membrane domain of closed complex I during turnover
+Supramolecule #1: Membrane domain of closed complex I during turnover
+Macromolecule #1: Mitochondrial complex I, 49 kDa subunit
+Macromolecule #2: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #3: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #4: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #5: Mitochondrial complex I, B14.7 subunit
+Macromolecule #6: NADH:ubiquinone oxidoreductase subunit B5
+Macromolecule #7: Acyl carrier protein
+Macromolecule #8: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #9: Mitochondrial complex I, PDSW subunit
+Macromolecule #10: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #11: NADH:ubiquinone oxidoreductase subunit S5
+Macromolecule #12: NADH:ubiquinone oxidoreductase subunit A3
+Macromolecule #13: NADH:ubiquinone oxidoreductase subunit B3
+Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #15: NADH:ubiquinone oxidoreductase subunit B4
+Macromolecule #16: Mitochondrial complex I, B16.6 subunit
+Macromolecule #17: Mitochondrial complex I, B17 subunit
+Macromolecule #18: NADH:ubiquinone oxidoreductase subunit B7
+Macromolecule #19: NADH:ubiquinone oxidoreductase subunit B9
+Macromolecule #20: NADH:ubiquinone oxidoreductase subunit B2
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #22: Mitochondrial complex I, ESSS subunit
+Macromolecule #23: Mitochondrial complex I, KFYI subunit
+Macromolecule #24: Mitochondrial complex I, MNLL subunit
+Macromolecule #25: Mitochondrial complex I, MWFE subunit
+Macromolecule #26: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #27: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #28: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #29: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #30: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
+Macromolecule #31: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #32: CARDIOLIPIN
+Macromolecule #33: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #34: ADENOSINE MONOPHOSPHATE
+Macromolecule #35: MYRISTIC ACID
+Macromolecule #36: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 3 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 100.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |