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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-11614 | |||||||||
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| Title | Plant mitochondrial respiratory complex I | |||||||||
Map data | Reconstruction of the plant mitochondrial respiratory complex I. | |||||||||
Sample |
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Keywords | Respiration / Complex I / mitochondria / plant / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationvegetative to reproductive phase transition of meristem / cold acclimation / Lyases; Carbon-oxygen lyases; Hydro-lyases / photorespiration / : / embryo development ending in seed dormancy / NADH dehydrogenase complex / response to abscisic acid / plant-type vacuole / ubiquinone biosynthetic process ...vegetative to reproductive phase transition of meristem / cold acclimation / Lyases; Carbon-oxygen lyases; Hydro-lyases / photorespiration / : / embryo development ending in seed dormancy / NADH dehydrogenase complex / response to abscisic acid / plant-type vacuole / ubiquinone biosynthetic process / cellular respiration / cobalt ion binding / response to osmotic stress / plastid / acyl carrier activity / oxidoreductase activity, acting on NAD(P)H / protein homotrimerization / NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase activity / response to salt stress / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / proton transmembrane transport / iron-sulfur cluster binding / aerobic respiration / carbonate dehydratase activity / respiratory electron transport chain / electron transport chain / chloroplast / mitochondrial intermembrane space / fatty acid biosynthetic process / NAD binding / mitochondrial membrane / FMN binding / 4 iron, 4 sulfur cluster binding / peroxisome / carbohydrate metabolic process / mitochondrial inner membrane / mitochondrial matrix / copper ion binding / nucleolus / protein-containing complex binding / mitochondrion / zinc ion binding / metal ion binding / extracellular region / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Soufari H / Waltz F / Hashem Y | |||||||||
| Funding support | France, 2 items
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Citation | Journal: Nat Commun / Year: 2020Title: Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM. Authors: Heddy Soufari / Camila Parrot / Lauriane Kuhn / Florent Waltz / Yaser Hashem / ![]() Abstract: Mitochondria are the powerhouses of eukaryotic cells and the site of essential metabolic reactions. Complex I or NADH:ubiquinone oxidoreductase is the main entry site for electrons into the ...Mitochondria are the powerhouses of eukaryotic cells and the site of essential metabolic reactions. Complex I or NADH:ubiquinone oxidoreductase is the main entry site for electrons into the mitochondrial respiratory chain and constitutes the largest of the respiratory complexes. Its structure and composition vary across eukaryote species. However, high resolution structures are available only for one group of eukaryotes, opisthokonts. In plants, only biochemical studies were carried out, already hinting at the peculiar composition of complex I in the green lineage. Here, we report several cryo-electron microscopy structures of the plant mitochondrial complex I. We describe the structure and composition of the plant respiratory complex I, including the ancestral mitochondrial domain composed of the carbonic anhydrase. We show that the carbonic anhydrase is a heterotrimeric complex with only one conserved active site. This domain is crucial for the overall stability of complex I as well as a peculiar lipid complex composed of cardiolipin and phosphatidylinositols. Moreover, we also describe the structure of one of the plant-specific complex I assembly intermediates, lacking the whole P module, in presence of the maturation factor GLDH. GLDH prevents the binding of the plant specific P1 protein, responsible for the linkage of the P to the P module. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_11614.map.gz | 166.8 MB | EMDB map data format | |
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| Header (meta data) | emd-11614-v30.xml emd-11614.xml | 56.4 KB 56.4 KB | Display Display | EMDB header |
| Images | emd_11614.png | 31.2 KB | ||
| Filedesc metadata | emd-11614.cif.gz | 13.5 KB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-11614 ftp://data.pdbj.org/pub/emdb/structures/EMD-11614 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7a23MC ![]() 7a24C C: citing same article ( M: atomic model generated by this map |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_11614.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Reconstruction of the plant mitochondrial respiratory complex I. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : Mitochondrial respiratory complex I
+Supramolecule #1: Mitochondrial respiratory complex I
+Macromolecule #1: 51kDa
+Macromolecule #2: Nad2m
+Macromolecule #3: Nad3m
+Macromolecule #4: Nad6m
+Macromolecule #5: Nad1m
+Macromolecule #6: Nad4Lm
+Macromolecule #7: PGIV
+Macromolecule #8: B16.6
+Macromolecule #9: MWFE
+Macromolecule #10: B9
+Macromolecule #11: B14.5a
+Macromolecule #12: B14.5b
+Macromolecule #13: 15kDa
+Macromolecule #14: Nad7m
+Macromolecule #15: 75kDa
+Macromolecule #16: 39kDa
+Macromolecule #17: Nad9m
+Macromolecule #18: 24kDa
+Macromolecule #19: 18kDa
+Macromolecule #20: 13kDa
+Macromolecule #21: B13
+Macromolecule #22: B17.2
+Macromolecule #23: PSST
+Macromolecule #24: TYKY
+Macromolecule #25: B14
+Macromolecule #26: 20.9kDa
+Macromolecule #27: B8
+Macromolecule #28: ACPM1
+Macromolecule #29: Unk1
+Macromolecule #30: P2
+Macromolecule #31: CAL1
+Macromolecule #32: CA1
+Macromolecule #33: Nad4m
+Macromolecule #34: PDSW
+Macromolecule #35: ESSS
+Macromolecule #36: B22
+Macromolecule #37: Nad5m
+Macromolecule #38: B18
+Macromolecule #39: AGGG
+Macromolecule #40: ACPM2
+Macromolecule #41: B15
+Macromolecule #42: Unk2
+Macromolecule #43: P1
+Macromolecule #44: B12-1
+Macromolecule #45: IRON/SULFUR CLUSTER
+Macromolecule #46: FLAVIN MONONUCLEOTIDE
+Macromolecule #47: Phosphatidylinositol
+Macromolecule #48: CARDIOLIPIN
+Macromolecule #49: UBIQUINONE-10
+Macromolecule #50: (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY...
+Macromolecule #51: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #52: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #53: ZINC ION
+Macromolecule #54: BICARBONATE ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL |
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| Buffer | pH: 7.5 |
| Grid | Model: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 20 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 45.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Keywords
Authors
France, 2 items
Citation
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