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Yorodumi- PDB-8b6h: Cryo-EM structure of cytochrome c oxidase dimer (complex IV) from... -
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-Basic information
Entry | Database: PDB / ID: 8b6h | |||||||||||||||
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Title | Cryo-EM structure of cytochrome c oxidase dimer (complex IV) from respiratory supercomplex of Tetrahymena thermophila | |||||||||||||||
Components |
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Keywords | ELECTRON TRANSPORT / Ciliate / mitochondrial / supercomplex | |||||||||||||||
Function / homology | Function and homology information dicarboxylic acid transmembrane transporter activity / protein maturation by [2Fe-2S] cluster transfer / : / cytochrome-c oxidase / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / electron transport coupled proton transport / ATP synthesis coupled electron transport / 2 iron, 2 sulfur cluster binding / protein transport ...dicarboxylic acid transmembrane transporter activity / protein maturation by [2Fe-2S] cluster transfer / : / cytochrome-c oxidase / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / electron transport coupled proton transport / ATP synthesis coupled electron transport / 2 iron, 2 sulfur cluster binding / protein transport / mitochondrial inner membrane / copper ion binding / DNA-binding transcription factor activity / heme binding / mitochondrion / membrane / nucleus / metal ion binding Similarity search - Function | |||||||||||||||
Biological species | Tetrahymena thermophila SB210 (eukaryote) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||||||||
Authors | Muhleip, A. / Kock Flygaard, R. / Amunts, A. | |||||||||||||||
Funding support | Sweden, European Union, 4items
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Citation | Journal: Nature / Year: 2023 Title: Structural basis of mitochondrial membrane bending by the I-II-III-IV supercomplex. Authors: Alexander Mühleip / Rasmus Kock Flygaard / Rozbeh Baradaran / Outi Haapanen / Thomas Gruhl / Victor Tobiasson / Amandine Maréchal / Vivek Sharma / Alexey Amunts / Abstract: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes ...Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III-IV supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization. #1: Journal: Biorxiv / Year: 2022 Title: Structural basis of mitochondrial membrane bending by I-II-III2-IV2 supercomplex Authors: Muhleip, A. / Flygaard, R.K. / Haapanen, O. / Baradaran, R. / Gruhl, T. / Tobiasson, V. / Marechal, A. / Sharma, V. / Amunts, A. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8b6h.cif.gz | 8.6 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8b6h.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8b6h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8b6h_validation.pdf.gz | 8 MB | Display | wwPDB validaton report |
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Full document | 8b6h_full_validation.pdf.gz | 8.5 MB | Display | |
Data in XML | 8b6h_validation.xml.gz | 653.4 KB | Display | |
Data in CIF | 8b6h_validation.cif.gz | 924.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b6/8b6h ftp://data.pdbj.org/pub/pdb/validation_reports/b6/8b6h | HTTPS FTP |
-Related structure data
Related structure data | 15867MC 8b6fC 8b6gC 8b6jC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Cytochrome c oxidase subunit ... , 3 types, 6 molecules DADaDBDbDDDd
#1: Protein | Mass: 80578.977 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q950Y4 #2: Protein | Mass: 72388.883 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q950Y9 #4: Protein | Mass: 75431.312 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23FF5 |
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+Protein , 34 types, 68 molecules DCDcDFDfDKDkDNDnDODoDPDpDQDqDSDsDUDuDVDvDWDwDXDxDYDyDZDzEAEa...
-Transmembrane protein, ... , 12 types, 24 molecules DEDeDGDgDHDhDJDjDMDmDRDrEBEbEHEhELElEMEmEOEoEQEq
#5: Protein | Mass: 15618.258 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: W7XCY5 #7: Protein | Mass: 12786.321 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23DS4 #8: Protein | Mass: 16427.672 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: I7MGF9 #10: Protein | Mass: 26601.174 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: W7WZP1 #12: Protein | Mass: 57814.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q22PJ5 #17: Protein | Mass: 41307.387 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23DG8 #27: Protein | Mass: 24701.131 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: I7LZX8 #33: Protein | Mass: 20388.264 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23D87 #37: Protein | Mass: 18801.604 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23VY4 #38: Protein | Mass: 18600.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q22DP8 #40: Protein | Mass: 15588.598 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23TE5 #42: Protein | Mass: 14344.524 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q22W32 |
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-NADH dehydrogenase [ubiquinone] 1 ... , 2 types, 4 molecules DIDiDTDt
#9: Protein | Mass: 28666.662 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: W7X287 #19: Protein | Mass: 37552.980 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q23DZ5 |
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-Zf-Tim10 DDP domain-containing ... , 2 types, 4 molecules ETEtEXEx
#45: Protein | Mass: 10435.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: Q231A8 #49: Protein | Mass: 8354.574 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila SB210 (eukaryote) / References: UniProt: W7XDM6 |
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-Non-polymers , 15 types, 245 molecules
#54: Chemical | ChemComp-HEA / #55: Chemical | #56: Chemical | #57: Chemical | ChemComp-CDL / #58: Chemical | ChemComp-PC1 / #59: Chemical | ChemComp-3PE / #60: Chemical | ChemComp-LPP / #61: Chemical | #62: Chemical | #63: Chemical | #64: Chemical | ChemComp-K / | #65: Chemical | ChemComp-UQ8 / #66: Chemical | #67: Chemical | ChemComp-FES / #68: Chemical | |
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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 |
-Sample preparation
Component | Name: Cytochrome c oxidase dimer (complex-IV) from respiratory supercomplex of Tetrahymena thermophila Type: COMPLEX / Entity ID: #1-#53 / Source: NATURAL |
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Molecular weight | Value: 3.2 MDa / Experimental value: NO |
Source (natural) | Organism: Tetrahymena thermophila (eukaryote) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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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 defocus max: 2600 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 25.66 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 138746 / Symmetry type: POINT | ||||||||||||||||||||||||
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