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Yorodumi- EMDB-28582: Structure of mitochondrial complex I from Drosophila melanogaster... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28582 | |||||||||
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Title | Structure of mitochondrial complex I from Drosophila melanogaster, Helix-locked state | |||||||||
Map data | ||||||||||
Sample |
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Keywords | NADH:ubiquinone oxidoreductase / TRANSLOCASE / OXIDOREDUCTASE | |||||||||
Function / homology | Function and homology information Mitochondrial protein import / Respiratory electron transport / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Protein lipoylation / Mitochondrial protein degradation / regulation of terminal button organization / Neutrophil degranulation / mitochondrial [2Fe-2S] assembly complex ...Mitochondrial protein import / Respiratory electron transport / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / RHOG GTPase cycle / Protein lipoylation / Mitochondrial protein degradation / regulation of terminal button organization / Neutrophil degranulation / mitochondrial [2Fe-2S] assembly complex / ubiquinone-6 biosynthetic process / cellular respiration / NADH:ubiquinone reductase (H+-translocating) / mitochondrial ATP synthesis coupled electron transport / respiratory chain complex I / : / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / acyl binding / acyl carrier activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / quinone binding / : / aerobic respiration / respiratory electron transport chain / proton transmembrane transport / reactive oxygen species metabolic process / determination of adult lifespan / response to reactive oxygen species / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / oxidoreductase activity / mitochondrial matrix / protein-containing complex binding / mitochondrion / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Drosophila melanogaster (fruit fly) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Padavannil A / Letts JA | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Elife / Year: 2023 Title: Resting mitochondrial complex I from adopts a helix-locked state. Authors: Abhilash Padavannil / Anjaneyulu Murari / Shauna-Kay Rhooms / Edward Owusu-Ansah / James A Letts / Abstract: Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the ...Respiratory complex I is a proton-pumping oxidoreductase key to bioenergetic metabolism. Biochemical studies have found a divide in the behavior of complex I in metazoans that aligns with the evolutionary split between Protostomia and Deuterostomia. Complex I from Deuterostomia including mammals can adopt a biochemically defined off-pathway 'deactive' state, whereas complex I from Protostomia cannot. The presence of off-pathway states complicates the interpretation of structural results and has led to considerable mechanistic debate. Here, we report the structure of mitochondrial complex I from the thoracic muscles of the model protostome . We show that although complex I (-CI) does not have a NEM-sensitive deactive state, it does show slow activation kinetics indicative of an off-pathway resting state. The resting-state structure of -CI from the thoracic muscle reveals multiple conformations. We identify a helix-locked state in which an N-terminal α-helix on the NDUFS4 subunit wedges between the peripheral and membrane arms. Comparison of the -CI structure and conformational states to those observed in bacteria, yeast, and mammals provides insight into the roles of subunits across organisms, explains why the -CI off-pathway resting state is NEM insensitive, and raises questions regarding current mechanistic models of complex I turnover. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28582.map.gz | 484 MB | EMDB map data format | |
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Header (meta data) | emd-28582-v30.xml emd-28582.xml | 63.4 KB 63.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_28582_fsc.xml | 16.9 KB | Display | FSC data file |
Images | emd_28582.png | 36.9 KB | ||
Filedesc metadata | emd-28582.cif.gz | 13.9 KB | ||
Others | emd_28582_half_map_1.map.gz emd_28582_half_map_2.map.gz | 474.4 MB 474.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28582 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28582 | HTTPS FTP |
-Validation report
Summary document | emd_28582_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_28582_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_28582_validation.xml.gz | 25.7 KB | Display | |
Data in CIF | emd_28582_validation.cif.gz | 33.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28582 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28582 | HTTPS FTP |
-Related structure data
Related structure data | 8eszMC 8eswC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_28582.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.88 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_28582_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_28582_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Mitochondrial complex I from the thoracic muscle of Drosophila me...
+Supramolecule #1: Mitochondrial complex I from the thoracic muscle of Drosophila me...
+Macromolecule #1: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #3: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
+Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
+Macromolecule #5: NADH dehydrogenase (Ubiquinone) 24 kDa subunit, isoform A
+Macromolecule #6: LD31474p
+Macromolecule #7: NADH dehydrogenase (ubiquinone) 23 kDa subunit
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #9: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #10: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #11: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #14: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
+Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
+Macromolecule #25: Acyl carrier protein, mitochondrial
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #28: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #29: NADH dehydrogenase (Ubiquinone) 39 kDa subunit, isoform A
+Macromolecule #30: GEO11417p1
+Macromolecule #31: Complex I-49kD
+Macromolecule #32: NADH dehydrogenase [ubiquinone] flavoprotein 3
+Macromolecule #33: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #34: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
+Macromolecule #36: RH45008p
+Macromolecule #37: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #38: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #39: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #40: NADH dehydrogenase (Ubiquinone) 13 kDa B subunit
+Macromolecule #41: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #43: CARDIOLIPIN
+Macromolecule #44: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
+Macromolecule #45: ZINC ION
+Macromolecule #46: IRON/SULFUR CLUSTER
+Macromolecule #47: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #48: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #49: UBIQUINONE-10
+Macromolecule #50: TETRADECANE
+Macromolecule #51: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #52: N-OCTANE
+Macromolecule #53: DODECANE
+Macromolecule #54: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #55: FLAVIN MONONUCLEOTIDE
+Macromolecule #56: (2R)-3-{[(S)-hydroxy(3-methylbutoxy)phosphoryl]oxy}-2-(octanoylox...
+Macromolecule #57: 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.7 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |