[English] 日本語
Yorodumi- PDB-8bef: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8bef | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI membrane core) | ||||||
Components |
| ||||||
Keywords | MEMBRANE PROTEIN / Plant / Mitochondria / Complex | ||||||
Function / homology | Function and homology information plastid outer membrane / TIM22 mitochondrial import inner membrane insertion complex / anther dehiscence / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / P450-containing electron transport chain / Lyases; Carbon-oxygen lyases; Hydro-lyases / NADH dehydrogenase complex / photorespiration / response to abscisic acid ...plastid outer membrane / TIM22 mitochondrial import inner membrane insertion complex / anther dehiscence / vegetative to reproductive phase transition of meristem / chloroplast outer membrane / P450-containing electron transport chain / Lyases; Carbon-oxygen lyases; Hydro-lyases / NADH dehydrogenase complex / photorespiration / response to abscisic acid / protein insertion into mitochondrial inner membrane / embryo development ending in seed dormancy / plant-type vacuole / regulation of reactive oxygen species metabolic process / porin activity / plastid / ubiquinone binding / pore complex / protein homotrimerization / NADH:ubiquinone reductase (H+-translocating) / NADH dehydrogenase activity / respiratory chain complex I / : / mitochondrial electron transport, NADH to ubiquinone / electron transport coupled proton transport / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / : / monoatomic ion transport / response to salt stress / aerobic respiration / chloroplast / carbonate dehydratase activity / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / peroxisome / mitochondrial outer membrane / mitochondrial inner membrane / copper ion binding / nucleolus / protein homodimerization activity / mitochondrion / extracellular region / identical protein binding / nucleus / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.13 Å | ||||||
Authors | Klusch, N. / Kuehlbrandt, W. | ||||||
Funding support | Germany, 1items
| ||||||
Citation | Journal: Nat Plants / Year: 2023 Title: 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. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8bef.cif.gz | 717.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8bef.ent.gz | 557.3 KB | Display | PDB format |
PDBx/mmJSON format | 8bef.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8bef_validation.pdf.gz | 3 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8bef_full_validation.pdf.gz | 3.1 MB | Display | |
Data in XML | 8bef_validation.xml.gz | 107.3 KB | Display | |
Data in CIF | 8bef_validation.cif.gz | 150.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/be/8bef ftp://data.pdbj.org/pub/pdb/validation_reports/be/8bef | HTTPS FTP |
-Related structure data
Related structure data | 16000MC 8bedC 8beeC 8behC 8belC 8bepC 8bpxC 8bq5C 8bq6C M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules AHJKLMN
#1: Protein | Mass: 13969.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: P92533, NADH:ubiquinone reductase (H+-translocating) |
---|---|
#2: Protein | Mass: 36020.070 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: B5TM92, NADH:ubiquinone reductase (H+-translocating) |
#3: Protein | Mass: 23690.385 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: A0A2P2CLG1, NADH:ubiquinone reductase (H+-translocating) |
#4: Protein | Mass: 11193.559 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: Q04614, NADH:ubiquinone reductase (H+-translocating) |
#5: Protein | Mass: 74497.977 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: B5TM94, NADH:ubiquinone reductase (H+-translocating) |
#6: Protein | Mass: 55995.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: P93313, NADH:ubiquinone reductase (H+-translocating) |
#7: Protein | Mass: 55486.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: O05000, NADH:ubiquinone reductase (H+-translocating) |
-Protein , 8 types, 8 molecules OYbdefix
#8: Protein | Mass: 17626.197 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: A0A384LA38 |
---|---|
#10: Protein | Mass: 17017.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: O48528 |
#13: Protein | Mass: 6810.177 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9ZPY5 |
#14: Protein | Mass: 9220.749 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q94AL6 |
#15: Protein | Mass: 9914.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9LZI6 |
#16: Protein | Mass: 11383.019 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q84W12 |
#17: Protein | Mass: 11808.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: A0A178W1I8 |
#20: Protein | Mass: 27985.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9SMN1 |
-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 3 types, 3 molecules XZa
#9: Protein | Mass: 11985.954 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q8LGE7 |
---|---|
#11: Protein | Mass: 16145.584 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q8RWA7 |
#12: Protein | Mass: 7349.628 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9C9Z5 |
-Uncharacterized protein ... , 2 types, 2 molecules uv
#18: Protein | Mass: 7546.790 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q8VZ65 |
---|---|
#19: Protein | Mass: 11965.520 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) / References: UniProt: Q9ZUX4 |
-Gamma carbonic anhydrase ... , 2 types, 2 molecules yz
#21: Protein | Mass: 30102.207 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: Q9C6B3, Lyases; Carbon-oxygen lyases; Hydro-lyases |
---|---|
#22: Protein | Mass: 30010.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Arabidopsis thaliana (thale cress) References: UniProt: Q9FWR5, Lyases; Carbon-oxygen lyases; Hydro-lyases |
-Non-polymers , 12 types, 1315 molecules
#23: Chemical | ChemComp-PGT / ( #24: Chemical | ChemComp-UQ9 / | #25: Chemical | ChemComp-PTY / #26: Chemical | ChemComp-Q7G / #27: Chemical | ChemComp-FE / | #28: Chemical | ChemComp-UQ5 / | #29: Chemical | #30: Chemical | #31: Chemical | #32: Chemical | ChemComp-ZN / | #33: Chemical | ChemComp-BCO / | #34: Water | ChemComp-HOH / | |
---|
-Details
Has ligand of interest | Y |
---|---|
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI membrane core) Type: COMPLEX / Entity ID: #1-#22 / Source: NATURAL |
---|---|
Source (natural) | Organism: Arabidopsis t (thale cress) |
Buffer solution | pH: 7.4 |
Specimen | Conc.: 0.18 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 70 % / Chamber temperature: 283.15 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 215000 X / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.20.1_4487: / Classification: refinement | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
EM software |
| ||||||||||||||||||||||||||||
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 1215138 | ||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.13 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 213993 / Symmetry type: POINT | ||||||||||||||||||||||||||||
Atomic model building | Space: REAL | ||||||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 9.89 Å2 | ||||||||||||||||||||||||||||
Refine LS restraints |
|