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- PDB-7q21: III2-IV2 respiratory supercomplex from Corynebacterium glutamicum -
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Open data
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Basic information
Entry | Database: PDB / ID: 7q21 | |||||||||||||||
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Title | III2-IV2 respiratory supercomplex from Corynebacterium glutamicum | |||||||||||||||
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![]() | ELECTRON TRANSPORT / MEMBRANE PROTEIN / CRYO-EM / RESPIRATORY SUPERCOMPLEX / ACTINOBACTERIA | |||||||||||||||
Function / homology | ![]() aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / : / electron transport coupled proton transport / ATP synthesis coupled electron transport / respiratory electron transport chain ...aerobic electron transport chain / cytochrome-c oxidase / oxidative phosphorylation / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / : / electron transport coupled proton transport / ATP synthesis coupled electron transport / respiratory electron transport chain / electron transport chain / 2 iron, 2 sulfur cluster binding / oxidoreductase activity / iron ion binding / copper ion binding / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||||||||
![]() | Kovalova, T. / Moe, A. / Krol, S. / Yanofsky, D.J. / Bott, M. / Sjostrand, D. / Rubinstein, J.L. / Hogbom, M. / Brzezinski, P. | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The respiratory supercomplex from C. glutamicum. Authors: Agnes Moe / Terezia Kovalova / Sylwia Król / David J Yanofsky / Michael Bott / Dan Sjöstrand / John L Rubinstein / Martin Högbom / Peter Brzezinski / ![]() ![]() ![]() Abstract: Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, ...Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, respiratory complexes III and IV form a CIIICIV supercomplex that catalyzes oxidation of menaquinol and reduction of dioxygen to water. We isolated the C. glutamicum supercomplex and used cryo-EM to determine its structure at 2.9 Å resolution. The structure shows a central CIII dimer flanked by a CIV on two sides. A menaquinone is bound in each of the Q and Q sites in each CIII and an additional menaquinone is positioned ∼14 Å from heme b. A di-heme cyt. cc subunit electronically connects each CIII with an adjacent CIV, with the Rieske iron-sulfur protein positioned with the iron near heme b. Multiple subunits interact to form a convoluted sub-structure at the cytoplasmic side of the supercomplex, which defines a path for proton transfer into CIV. | |||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 990.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.6 MB | Display | ![]() |
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Full document | ![]() | 3.7 MB | Display | |
Data in XML | ![]() | 158.2 KB | Display | |
Data in CIF | ![]() | 205 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 13777MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Protein , 5 types, 10 molecules YyFfAaVvKk
#1: Protein | Mass: 8188.084 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() #4: Protein | Mass: 15557.285 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: ctaF, Cgl2194, cg2408 Production host: ![]() References: UniProt: Q8NNK3, cytochrome-c oxidase #7: Protein | Mass: 45232.207 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: qcrA, Cgl2190, cg2404 Production host: ![]() References: UniProt: Q79VE8 #13: Protein | Mass: 8373.271 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: Cgl0818 Production host: ![]() References: UniProt: Q8NS61 #14: Protein | Mass: 6628.905 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: Cgl0673 Production host: ![]() References: UniProt: Q8NSJ8 |
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-Cytochrome c oxidase subunit ... , 3 types, 6 molecules EeGgDd
#2: Protein | Mass: 22457.217 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: ctaE, Cgl2192, cg2406 Production host: ![]() References: UniProt: Q9AEL8, cytochrome-c oxidase #5: Protein | Mass: 39665.562 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: ctaC, Cgl2195, cg2409 Production host: ![]() References: UniProt: Q8NNK2, cytochrome-c oxidase #6: Protein | Mass: 66340.164 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: ctaD, Cgl2523, cg2780 Production host: ![]() References: UniProt: Q79VD7, cytochrome-c oxidase |
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-Uncharacterized ... , 2 types, 4 molecules HhLl
#3: Protein | Mass: 16385.588 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: Cgl2017, cg2211 Production host: ![]() References: UniProt: Q8NP09 #8: Protein | Mass: 20025.750 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: Cgl2664, cg2949 Production host: ![]() References: UniProt: Q8NMB4 |
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-Cytochrome bc1 complex cytochrome ... , 2 types, 4 molecules BbCc
#9: Protein | Mass: 59863.699 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: qcrB, Cgl2189, cg2403 Production host: ![]() References: UniProt: Q79VE9, quinol-cytochrome-c reductase #10: Protein | Mass: 29898.850 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: qcrC, Cgl2191, cg2405 Production host: ![]() References: UniProt: Q8NNK5, quinol-cytochrome-c reductase |
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-Co-purified unknown peptide built as polyALA ... , 2 types, 2 molecules Xx
#11: Protein/peptide | Mass: 1823.254 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
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#12: Protein/peptide | Mass: 1908.359 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
-Non-polymers , 15 types, 92 molecules ![](data/chem/img/CDL.gif)
![](data/chem/img/7PH.gif)
![](data/chem/img/TRD.gif)
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![](data/chem/img/HAS.gif)
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![](data/chem/img/MQ9.gif)
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![](data/chem/img/PLM.gif)
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![](data/chem/img/HEC.gif)
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![](data/chem/img/TRD.gif)
![](data/chem/img/9XX.gif)
![](data/chem/img/TWT.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/HAS.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/FES.gif)
![](data/chem/img/MQ9.gif)
![](data/chem/img/9YF.gif)
![](data/chem/img/PLM.gif)
![](data/chem/img/HEM.gif)
![](data/chem/img/HEC.gif)
#15: Chemical | ChemComp-CDL / #16: Chemical | ChemComp-7PH / ( #17: Chemical | ChemComp-TRD / #18: Chemical | ChemComp-9XX / ( #19: Chemical | #20: Chemical | ChemComp-CU / #21: Chemical | #22: Chemical | ChemComp-HAS / #23: Chemical | #24: Chemical | #25: Chemical | ChemComp-MQ9 / #26: Chemical | ChemComp-9YF / ( #27: Chemical | ChemComp-PLM / #28: Chemical | ChemComp-HEM / #29: Chemical | ChemComp-HEC / |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: The respiratory supercomplex / Type: COMPLEX / Entity ID: #1-#14 / Source: RECOMBINANT |
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Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: YES |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Conc.: 10 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: C-flat-2/2 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 276 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
Image recording | Average exposure time: 8 sec. / Electron dose: 55 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: REFMAC / Version: 5.8.0257 / Classification: refinement | ||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||
3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 65391 / Symmetry type: POINT | ||||||||||||||||
Refinement | Resolution: 3→328.6 Å / Cor.coef. Fo:Fc: 0.799
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Displacement parameters | Biso mean: 56.633 Å2
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LS refinement shell | Highest resolution: 3 Å /
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