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Yorodumi- EMDB-16172: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -
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Basic information
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| Title | Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (Complete conformation 2 composition) | |||||||||
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Keywords | Plant / Mitochondria / Complex / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationplastid outer membrane / anther dehiscence / TIM22 mitochondrial import inner membrane insertion complex / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / cold acclimation / mitochondrial processing peptidase / Lyases; Carbon-oxygen lyases; Hydro-lyases / P450-containing electron transport chain / plant-type cell wall ...plastid outer membrane / anther dehiscence / TIM22 mitochondrial import inner membrane insertion complex / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / cold acclimation / mitochondrial processing peptidase / Lyases; Carbon-oxygen lyases; Hydro-lyases / P450-containing electron transport chain / plant-type cell wall / photorespiration / protein insertion into mitochondrial inner membrane / embryo development ending in seed dormancy / NADH dehydrogenase complex / response to abscisic acid / plant-type vacuole / vacuole / respiratory chain complex III / quinol-cytochrome-c reductase / cobalt ion binding / quinol-cytochrome-c reductase activity / response to osmotic stress / regulation of reactive oxygen species metabolic process / plastid / mitochondrial electron transport, ubiquinol to cytochrome c / porin activity / pore complex / protein homotrimerization / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / monoatomic ion transport / response to salt stress / proton transmembrane transport / chloroplast / respiratory electron transport chain / carbonate dehydratase activity / electron transport chain / mitochondrial membrane / metalloendopeptidase activity / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / NAD binding / fatty acid biosynthetic process / peroxisome / FMN binding / 4 iron, 4 sulfur cluster binding / carbohydrate metabolic process / mitochondrial outer membrane / electron transfer activity / oxidoreductase activity / mitochondrial inner membrane / mitochondrial matrix / copper ion binding / heme binding / nucleolus / protein homodimerization activity / mitochondrion / proteolysis / extracellular region / zinc ion binding / ATP binding / metal ion binding / identical protein binding / nucleus / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Klusch N / Kuehlbrandt W | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: Nat Plants / Year: 2023Title: Cryo-EM structure of the respiratory I + III supercomplex from Arabidopsis thaliana at 2 Å resolution. Authors: Niklas Klusch / Maximilian Dreimann / Jennifer Senkler / Nils Rugen / Werner Kühlbrandt / Hans-Peter Braun / ![]() Abstract: Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis ...Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III with a co-purified ubiquinone in the Q site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_16172.map.gz | 99 MB | EMDB map data format | |
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| Header (meta data) | emd-16172-v30.xml emd-16172.xml | 77.6 KB 77.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_16172_fsc.xml | 26.6 KB | Display | FSC data file |
| Images | emd_16172.png | 186.9 KB | ||
| Filedesc metadata | emd-16172.cif.gz | 16.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16172 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16172 | HTTPS FTP |
-Validation report
| Summary document | emd_16172_validation.pdf.gz | 452.7 KB | Display | EMDB validaton report |
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| Full document | emd_16172_full_validation.pdf.gz | 452.2 KB | Display | |
| Data in XML | emd_16172_validation.xml.gz | 20.8 KB | Display | |
| Data in CIF | emd_16172_validation.cif.gz | 29.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16172 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16172 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8bq6MC ![]() 8bedC ![]() 8beeC ![]() 8befC ![]() 8behC ![]() 8belC ![]() 8bepC ![]() 8bpxC ![]() 8bq5C C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_16172.map.gz / Format: CCP4 / Size: 1.6 GB / 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: 0.573 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete ...
+Supramolecule #1: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (Complete ...
+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
+Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2
+Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
+Macromolecule #6: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
+Macromolecule #7: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
+Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1
+Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
+Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6
+Macromolecule #11: NADH dehydrogenase subunit 4L
+Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5
+Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4
+Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2
+Macromolecule #15: AT3G07480.1
+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 1, mitochondrial
+Macromolecule #21: Acyl carrier protein 2, mitochondrial
+Macromolecule #22: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun...
+Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
+Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8-B
+Macromolecule #25: Outer envelope pore protein 16-3, chloroplastic/mitochondrial
+Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
+Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
+Macromolecule #28: At2g46540/F11C10.23
+Macromolecule #29: Transmembrane protein
+Macromolecule #30: Excitatory amino acid transporter
+Macromolecule #31: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5-B
+Macromolecule #32: At4g16450
+Macromolecule #33: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein
+Macromolecule #34: P1
+Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2
+Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3-A
+Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...
+Macromolecule #38: B15 -- 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-B
+Macromolecule #42: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
+Macromolecule #43: Uncharacterized protein At1g67785
+Macromolecule #44: Uncharacterized protein At2g27730, mitochondrial
+Macromolecule #45: Gamma carbonic anhydrase-like 2, mitochondrial
+Macromolecule #46: Gamma carbonic anhydrase 2, mitochondrial
+Macromolecule #47: Gamma carbonic anhydrase 1, mitochondrial
+Macromolecule #48: Probable mitochondrial-processing peptidase subunit alpha-1, mito...
+Macromolecule #49: Probable mitochondrial-processing peptidase subunit beta, mitocho...
+Macromolecule #50: Cytochrome b
+Macromolecule #51: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
+Macromolecule #52: Cytochrome c1 2, heme protein, mitochondrial
+Macromolecule #53: Cytochrome b-c1 complex subunit 7-2, mitochondrial
+Macromolecule #54: Cytochrome b-c1 complex subunit 8-1, mitochondrial
+Macromolecule #55: Cytochrome b-c1 complex subunit 6-1, mitochondrial
+Macromolecule #56: Cytochrome b-c1 complex subunit 9, mitochondrial
+Macromolecule #57: Cytochrome b-c1 complex subunit 10, mitochondrial
+Macromolecule #58: IRON/SULFUR CLUSTER
+Macromolecule #59: FE2/S2 (INORGANIC) CLUSTER
+Macromolecule #60: FLAVIN MONONUCLEOTIDE
+Macromolecule #61: Ubiquinone-9
+Macromolecule #62: FE (III) ION
+Macromolecule #63: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
+Macromolecule #64: ZINC ION
+Macromolecule #65: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...
+Macromolecule #66: CROTONYL COENZYME A
+Macromolecule #67: PROTOPORPHYRIN IX CONTAINING FE
+Macromolecule #68: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14...
+Macromolecule #69: UBIQUINONE-7
-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 | 0.18 mg/mL |
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| Buffer | pH: 7.4 |
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - #0 - Film type ID: 1 / Support film - #0 - Material: CARBON / Support film - #0 - topology: CONTINUOUS / Support film - #1 - Film type ID: 2 / Support film - #1 - Material: GRAPHENE / Support film - #1 - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 70 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 215000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL |
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| Output model | ![]() PDB-8bq6: |
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Keywords
Authors
Germany, 1 items
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FIELD EMISSION GUN


