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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-4356 | ||||||||||||
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| Title | Mouse mitochondrial complex I in the deactive state | ||||||||||||
Map data | Mouse mitochondrial complex I in the deactive state | ||||||||||||
Sample |
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Keywords | Complex I / mitochondria / proton pump / membrane protein / oxidoreductase | ||||||||||||
| Function / homology | Function and homology informationMitochondrial protein import / response to injury involved in regulation of muscle adaptation / mesenchymal stem cell proliferation / reproductive system development / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination ...Mitochondrial protein import / response to injury involved in regulation of muscle adaptation / mesenchymal stem cell proliferation / reproductive system development / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / RHOG GTPase cycle / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / Respiratory electron transport / protein insertion into mitochondrial inner membrane / circulatory system development / mesenchymal stem cell differentiation / response to light intensity / blastocyst hatching / respiratory system process / Mitochondrial protein degradation / iron-sulfur cluster assembly complex / psychomotor behavior / adult walking behavior / mitochondrial ATP synthesis coupled electron transport / protein lipoylation / stem cell division / cellular response to oxygen levels / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / ubiquinone biosynthetic process / respiratory chain complex / neural precursor cell proliferation / gliogenesis / negative regulation of non-canonical NF-kappaB signal transduction / cellular respiration / cardiac muscle tissue development / response to hydroperoxide / positive regulation of mitochondrial membrane potential / oxygen sensor activity / [2Fe-2S] cluster assembly / cellular response to glucocorticoid stimulus / iron-sulfur cluster assembly / adult behavior / dopamine metabolic process / NADH:ubiquinone reductase (H+-translocating) / ubiquinone binding / positive regulation of ATP biosynthetic process / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / electron transport coupled proton transport / acyl binding / mitochondrial respiratory chain complex I assembly / oxidoreductase activity, acting on NAD(P)H / NADH dehydrogenase activity / neuron development / respiratory chain complex I / positive regulation of execution phase of apoptosis / NADH dehydrogenase (ubiquinone) activity / response to cAMP / acyl carrier activity / extrinsic apoptotic signaling pathway / cellular response to interferon-beta / quinone binding / cellular response to retinoic acid / ATP synthesis coupled electron transport / tricarboxylic acid cycle / negative regulation of reactive oxygen species biosynthetic process / neurogenesis / cerebellum development / multicellular organism growth / Neutrophil degranulation / reactive oxygen species metabolic process / muscle contraction / response to hormone / kidney development / visual perception / fatty acid metabolic process / ionotropic glutamate receptor binding / regulation of mitochondrial membrane potential / aerobic respiration / DNA damage response, signal transduction by p53 class mediator / respiratory electron transport chain / response to hydrogen peroxide / response to nicotine / synaptic membrane / mitochondrion organization / response to cocaine / monooxygenase activity / sensory perception of sound / brain development / circadian rhythm / electron transport chain / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / cognition / cellular senescence / NAD binding / mitochondrial membrane / positive regulation of protein catabolic process / gene expression / FMN binding / in utero embryonic development Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||||||||
Authors | Agip ANA / Blaza JN | ||||||||||||
| Funding support | United Kingdom, 3 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2018Title: Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states. Authors: Ahmed-Noor A Agip / James N Blaza / Hannah R Bridges / Carlo Viscomi / Shaun Rawson / Stephen P Muench / Judy Hirst / ![]() Abstract: Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian ...Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I. | ||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
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Downloads & links
-EMDB archive
| Map data | emd_4356.map.gz | 172 MB | EMDB map data format | |
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| Header (meta data) | emd-4356-v30.xml emd-4356.xml | 70.5 KB 70.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_4356_fsc.xml | 12.9 KB | Display | FSC data file |
| Images | emd_4356.png | 97.2 KB | ||
| Filedesc metadata | emd-4356.cif.gz | 14.3 KB | ||
| Others | emd_4356_half_map_1.map.gz emd_4356_half_map_2.map.gz | 146.1 MB 146 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4356 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4356 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6g72MC ![]() 4345C ![]() 6g2jC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | |
| EM raw data | EMPIAR-10604 (Title: Single particle cryo-EM dataset of Mus musculus mitochondrial complex I in the deactive stateData size: 2.7 TB Data #1: Single particle cryo-EM dataset of Mus musculus mitochondrial complex I in the deactive state [micrographs - multiframe]) |
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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_4356.map.gz / Format: CCP4 / Size: 184 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Mouse mitochondrial complex I in the deactive state | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.33 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: Half-1
| File | emd_4356_half_map_1.map | ||||||||||||
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| Annotation | Half-1 | ||||||||||||
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| Density Histograms |
-Half map: Half-2
| File | emd_4356_half_map_2.map | ||||||||||||
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| Annotation | Half-2 | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Mitochondrial complex I from mouse in the deactive state
+Supramolecule #1: Mitochondrial complex I from mouse in the deactive state
+Macromolecule #1: NADH-ubiquinone oxidoreductase chain 3
+Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
+Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
+Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
+Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #6: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #7: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
+Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L
+Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...
+Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...
+Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
+Macromolecule #18: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
+Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
+Macromolecule #20: Acyl carrier protein, mitochondrial
+Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
+Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
+Macromolecule #24: MCG5603
+Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
+Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
+Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 subunit C2
+Macromolecule #30: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
+Macromolecule #31: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
+Macromolecule #32: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...
+Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...
+Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
+Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...
+Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
+Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
+Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
+Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
+Macromolecule #41: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
+Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
+Macromolecule #44: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
+Macromolecule #45: IRON/SULFUR CLUSTER
+Macromolecule #46: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #47: FLAVIN MONONUCLEOTIDE
+Macromolecule #48: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #49: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #50: ZINC ION
+Macromolecule #51: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...
+Macromolecule #52: ACETYL GROUP
-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 | 3 mg/mL | ||||||||||||
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| Buffer | pH: 7.14 Component:
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| Grid | Model: Quantifoil UltrAuFoil / Material: GOLD / Mesh: 300 Details: Gold was PEGylated prior to use in anaerobic ethanol in 5mM SPT-11P6 (Sensopath Technologies) for two days 0.6/1 holes | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: 8-16s blotting.. | ||||||||||||
| Details | Peak fraction from a gel filtration column- monodisperse and not concentrated. The complex was put into the deactive state by heating at 37degC for 30 mins before isolation in detergent. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Lower energy threshold: 0 eV / Energy filter - Upper energy threshold: 20 eV |
| Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-30 / Number grids imaged: 1 / Average exposure time: 15.0 sec. / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Calibrated magnification: 37600 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.4 µm / Nominal defocus min: 2.2 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Details | Used default paramteres in phenix.real_space_refine |
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| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
| Output model | ![]() PDB-6g72: |
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About Yorodumi



Keywords
Authors
United Kingdom, 3 items
Citation
UCSF Chimera











































Z (Sec.)
Y (Row.)
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