+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15216 | |||||||||
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Title | Complex I inhibited by rotenone open3 | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Ovis aries (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
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_15216.map.gz | 27.7 MB | EMDB map data format | |
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Header (meta data) | emd-15216-v30.xml emd-15216.xml | 11.6 KB 11.6 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_15216_fsc.xml | 17.7 KB | Display | FSC data file |
Images | emd_15216.png | 174.5 KB | ||
Others | emd_15216_half_map_1.map.gz emd_15216_half_map_2.map.gz | 391.3 MB 391.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15216 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15216 | HTTPS FTP |
-Related structure data
Related structure data | 6zk9C 6zkaC 6zkbC 6zkcC 6zkdC 6zkeC 6zkfC 6zkgC 6zkhC 6zkiC 6zkjC 6zkkC 6zklC 6zkmC 6zknC 6zkoC 6zkpC 6zkqC 6zkrC 6zksC 6zktC 6zkuC 6zkvC C: citing same article (ref.) |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_15216.map.gz / Format: CCP4 / Size: 29.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.061 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_15216_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_15216_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Complex I inhibited by rotenone, open3
Entire | Name: Complex I inhibited by rotenone, open3 |
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Components |
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-Supramolecule #1: Complex I inhibited by rotenone, open3
Supramolecule | Name: Complex I inhibited by rotenone, open3 / type: complex / Chimera: Yes / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Ovis aries (sheep) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 100.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |