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Open data
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Basic information
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| Title | Substrate-engaged TOM complex from yeast | |||||||||
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Sample |
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Keywords | Mitochondrial protein import / TOM / protein translocation / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationmitochondrial outer membrane translocase complex assembly / mitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / protein transmembrane transport / : / porin activity / pore complex / protein import into mitochondrial matrix / transmembrane protein transporter activity / monoatomic ion transport ...mitochondrial outer membrane translocase complex assembly / mitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / protein transmembrane transport / : / porin activity / pore complex / protein import into mitochondrial matrix / transmembrane protein transporter activity / monoatomic ion transport / intracellular protein transport / mitochondrial intermembrane space / mitochondrial outer membrane / mitochondrion / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.94 Å | |||||||||
Authors | Yang YQ / Wang GP / Wang SS | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2025Title: Dynamic TOM-TIM23 supercomplex directs mitochondrial protein translocation and sorting. Authors: Yuqi Yang / Shanshan Wang / Guopeng Wang / Yuke Lian / Lingfeng Xue / Wenhong Jiang / Qiang Guo / Chen Song / Long Li / ![]() Abstract: The mitochondrial translocase of the outer membrane (TOM) and translocase of the inner membrane 23 (TIM23) complexes are coupled to control protein import across the outer and inner membranes, ...The mitochondrial translocase of the outer membrane (TOM) and translocase of the inner membrane 23 (TIM23) complexes are coupled to control protein import across the outer and inner membranes, respectively. However, the mechanisms of protein recognition and sorting in the TOM-TIM23 pathway remain unclear. Here we report cryo-electron microscopy structures of a translocating polypeptide substrate captured in the active TOM-TIM23 supercomplex from Saccharomyces cerevisiae. In the TOM complex, the polypeptide substrate adopts multiple conformations stabilized by hydrophilic residues from distinct regions of the Tom40 channel. In the TIM23 complex, the Tim17 and Mgr2 subunits create the translocation pathway, with a central restriction formed by four highly conserved hydrophobic residues. The substrate primarily interacts with hydrophobic residues along the Tim17-Mgr2 pathway. Substrate hydrophobicity modulates the association of Mgr2 with Tim17, enabling dynamic regulation of protein sorting toward either the matrix or membrane. These findings reveal a sophisticated translocation mechanism of the TOM-TIM23 supercomplex that ensures the efficient import of diverse mitochondrial proteins. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_61256.map.gz | 7.8 MB | EMDB map data format | |
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| Header (meta data) | emd-61256-v30.xml emd-61256.xml | 24.2 KB 24.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_61256_fsc.xml | 10.6 KB | Display | FSC data file |
| Images | emd_61256.png | 69.2 KB | ||
| Filedesc metadata | emd-61256.cif.gz | 6.8 KB | ||
| Others | emd_61256_half_map_1.map.gz emd_61256_half_map_2.map.gz | 80.5 MB 80.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-61256 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-61256 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9j99MC ![]() 9j9bC M: atomic model generated by this map C: citing same article ( |
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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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Map
| File | Download / File: emd_61256.map.gz / Format: CCP4 / Size: 103 MB / 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: 0.95 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_61256_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_61256_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Substrate-engaged TOM complex from yeast
| Entire | Name: Substrate-engaged TOM complex from yeast |
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| Components |
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-Supramolecule #1: Substrate-engaged TOM complex from yeast
| Supramolecule | Name: Substrate-engaged TOM complex from yeast / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Mitochondrial import receptor subunit TOM40
| Macromolecule | Name: Mitochondrial import receptor subunit TOM40 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 42.071141 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSAPTPLAEA SQIPTIPALS PLTAKQSKGN FFSSNPISSF VVDTYKQLHS HRQSLELVNP GTVENLNKEV SRDVFLSQYF FTGLRADLN KAFSMNPAFQ TSHTFSIGSQ ALPKYAFSAL FANDNLFAQG NIDNDLSVSG RLNYGWDKKN ISKVNLQISD G QPTMCQLE ...String: MSAPTPLAEA SQIPTIPALS PLTAKQSKGN FFSSNPISSF VVDTYKQLHS HRQSLELVNP GTVENLNKEV SRDVFLSQYF FTGLRADLN KAFSMNPAFQ TSHTFSIGSQ ALPKYAFSAL FANDNLFAQG NIDNDLSVSG RLNYGWDKKN ISKVNLQISD G QPTMCQLE QDYQASDFSV NVKTLNPSFS EKGEFTGVAV ASFLQSVTPQ LALGLETLYS RTDGSAPGDA GVSYLTRYVS KK QDWIFSG QLQANGALIA SLWRKVAQNV EAGIETTLQA GMVPITDPLM GTPIGIQPTV EGSTTIGAKY EYRQSVYRGT LDS NGKVAC FLERKVLPTL SVLFCGEIDH FKNDTKIGCG LQFETAGNQE LLMLQQGLDA DGNPLQALPQ L UniProtKB: Mitochondrial import receptor subunit TOM40 |
-Macromolecule #2: Mitochondrial import receptor subunit TOM22
| Macromolecule | Name: Mitochondrial import receptor subunit TOM22 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 16.801373 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MVELTEIKDD VVQLDEPQFS RNQAIVEEKA SATNNDVVDD EDDSDSDFED EFDENETLLD RIVALKDIVP PGKRQTISNF FGFTSSFVR NAFTKSGNLA WTLTTTALLL GVPLSLSILA EQQLIEMEKT FDLQSDANNI LAQGEKDAAA TAN UniProtKB: Mitochondrial import receptor subunit TOM22 |
-Macromolecule #3: Mitochondrial import receptor subunit TOM5
| Macromolecule | Name: Mitochondrial import receptor subunit TOM5 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.993924 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MFGLPQQEVS EEEKRAHQEQ TEKTLKQAAY VAAFLWVSPM IWHLVKKQWK UniProtKB: Mitochondrial import receptor subunit TOM5 |
-Macromolecule #4: Mitochondrial import receptor subunit TOM6
| Macromolecule | Name: Mitochondrial import receptor subunit TOM6 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 6.41046 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MDGMFAMPGA AAGAASPQQP KSRFQAFKES PLYTIALNGA FFVAGVAFIQ SPLMDMLAPQ L UniProtKB: Mitochondrial import receptor subunit TOM6 |
-Macromolecule #5: Mitochondrial import receptor subunit TOM7
| Macromolecule | Name: Mitochondrial import receptor subunit TOM7 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 6.876955 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSFLPSFILS DESKERISKI LTLTHNVAHY GWIPFVLYLG WAHTSNRPNF LNLLSPLPSV UniProtKB: Mitochondrial import receptor subunit TOM7 |
-Macromolecule #6: UNDECANE
| Macromolecule | Name: UNDECANE / type: ligand / ID: 6 / Number of copies: 26 / Formula: UND |
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| Molecular weight | Theoretical: 156.308 Da |
| Chemical component information | ![]() ChemComp-UND: |
-Macromolecule #7: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
| Macromolecule | Name: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 7 / Number of copies: 25 / Formula: PC1 |
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| Molecular weight | Theoretical: 790.145 Da |
| Chemical component information | ![]() ChemComp-PC1: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE |
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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: 60.0 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: 1.6 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 130000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation


Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

