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Open data
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Basic information
| Entry | Database: PDB / ID: 7vc9 | |||||||||||||||||||||||||||
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| Title | Tom20 subunits | |||||||||||||||||||||||||||
Components | Mitochondrial import receptor subunit TOM20 homolog | |||||||||||||||||||||||||||
Keywords | TRANSLOCASE / Tom20 / Cryo-EM | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationtRNA import into mitochondrion / TOM complex / mitochondrion targeting sequence binding / mitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / mitochondria-associated endoplasmic reticulum membrane contact site / migrasome / protein-transporting ATPase activity / Mitochondrial protein import / protein targeting to mitochondrion ...tRNA import into mitochondrion / TOM complex / mitochondrion targeting sequence binding / mitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / mitochondria-associated endoplasmic reticulum membrane contact site / migrasome / protein-transporting ATPase activity / Mitochondrial protein import / protein targeting to mitochondrion / protein import into mitochondrial matrix / sperm midpiece / PINK1-PRKN Mediated Mitophagy / cell periphery / unfolded protein binding / mitochondrial outer membrane / Ub-specific processing proteases / mitochondrion Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 13 Å | |||||||||||||||||||||||||||
Authors | Liu, D.S. / Sui, S.F. | |||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2022Title: Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors. Authors: Jiayue Su / Desheng Liu / Fan Yang / Mei-Qing Zuo / Chang Li / Meng-Qiu Dong / Shan Sun / Sen-Fang Sui / ![]() Abstract: Mitochondrial preproteins synthesized in cytosol are imported into mitochondria by a multisubunit translocase of the outer membrane (TOM) complex. Functioned as the receptor, the TOM complex ...Mitochondrial preproteins synthesized in cytosol are imported into mitochondria by a multisubunit translocase of the outer membrane (TOM) complex. Functioned as the receptor, the TOM complex components, Tom 20, Tom22, and Tom70, recognize the presequence and further guide the protein translocation. Their deficiency has been linked with neurodegenerative diseases and cardiac pathology. Although several structures of the TOM complex have been reported by cryoelectron microscopy (cryo-EM), how Tom22 and Tom20 function as TOM receptors remains elusive. Here we determined the structure of TOM core complex at 2.53 Å and captured the structure of the TOM complex containing Tom22 and Tom20 cytosolic domains at 3.74 Å. Structural analysis indicates that Tom20 and Tom22 share a similar three-helix bundle structural feature in the cytosolic domain. Further structure-guided biochemical analysis reveals that the Tom22 cytosolic domain is responsible for binding to the presequence, and the helix H1 is critical for this binding. Altogether, our results provide insights into the functional mechanism of the TOM complex recognizing and transferring preproteins across the mitochondrial membrane. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7vc9.cif.gz | 70.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7vc9.ent.gz | 52.6 KB | Display | PDB format |
| PDBx/mmJSON format | 7vc9.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7vc9_validation.pdf.gz | 725.7 KB | Display | wwPDB validaton report |
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| Full document | 7vc9_full_validation.pdf.gz | 729.2 KB | Display | |
| Data in XML | 7vc9_validation.xml.gz | 13 KB | Display | |
| Data in CIF | 7vc9_validation.cif.gz | 18.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vc/7vc9 ftp://data.pdbj.org/pub/pdb/validation_reports/vc/7vc9 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31889MC ![]() 7vd2C ![]() 7vddC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 16319.862 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TOMM20, KIAA0016 / Production host: Homo sapiens (human) / References: UniProt: Q15388Has protein modification | N | |
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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 translocase of the outer mitochondrial membrane of Tom20 subunit Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| EM embedding | Material: Digitonin |
| Vitrification | Cryogen name: ETHANE |
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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 |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.18.2_3874: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 13 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 347600 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
China, 1items
Citation




PDBj


gel filtration
