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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Human TOM-TIM22 supercomplex with substrate GGC1-sfGFP | |||||||||
Map data | Human TOM-TIM22 supercomplex with GGC1-sfGFP | |||||||||
Sample |
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Keywords | Mitochondria / Protein translocation / TRANSLOCASE | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 12.37 Å | |||||||||
Authors | Liu XL / Cai HJ / Li L | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2026Title: Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import. Authors: Xiaolong Liu / Hongjun Cai / Hao Wang / Xueyin Zhou / Yutong Zhang / Shuai Liu / Jiajun Zhu / Long Li / ![]() Abstract: Metabolite carriers that control essential metabolite transport are imported into mitochondria through the TOM and TIM22 complexes. How TOM and TIM22 coordinate in human mitochondria has remained ...Metabolite carriers that control essential metabolite transport are imported into mitochondria through the TOM and TIM22 complexes. How TOM and TIM22 coordinate in human mitochondria has remained largely unknown. Here we show that human TOM and TIM22 assemble into a supercomplex that seamlessly couples carrier translocation across the outer and inner membranes, unlike in yeast where the two complexes appear to function separately. Cryo-electron microscopy structures of the human TOM-TIM22 supercomplex reveal unpaired carrier transmembrane segments traversing the TOM channel along a hydrophobic path and exiting through an unexpected lateral groove outside the channel. The membrane-bound small Tim subunits provide the substrate entry site for TIM22, while a membrane-exposed groove of TIM22 serves as the exit for carrier insertion into the inner membrane. These findings provide insights into the human carrier translocation pathway at molecular resolution and establish the TOM-TIM22 supercomplex as a central organizing unit of mitochondrial carrier import. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_66278.map.gz | 242.2 MB | EMDB map data format | |
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| Header (meta data) | emd-66278-v30.xml emd-66278.xml | 17.4 KB 17.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_66278_fsc.xml | 17.2 KB | Display | FSC data file |
| Images | emd_66278.png | 57.2 KB | ||
| Filedesc metadata | emd-66278.cif.gz | 4.7 KB | ||
| Others | emd_66278_half_map_1.map.gz emd_66278_half_map_2.map.gz | 474.6 MB 474.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-66278 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-66278 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_66278.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Human TOM-TIM22 supercomplex with GGC1-sfGFP | ||||||||||||||||||||||||||||||||||||
| 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: Human TOM-TIM22 supercomplex with GGC1-sfGFP half map 1
| File | emd_66278_half_map_1.map | ||||||||||||
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| Annotation | Human TOM-TIM22 supercomplex with GGC1-sfGFP half map 1 | ||||||||||||
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| Density Histograms |
-Half map: Human TOM-TIM22 supercomplex with GGC1-sfGFP half map 2
| File | emd_66278_half_map_2.map | ||||||||||||
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| Annotation | Human TOM-TIM22 supercomplex with GGC1-sfGFP half map 2 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Human TOM-TIM22 supercomplex with substrate GGC1-sfGFP
| Entire | Name: Human TOM-TIM22 supercomplex with substrate GGC1-sfGFP |
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| Components |
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-Supramolecule #1: Human TOM-TIM22 supercomplex with substrate GGC1-sfGFP
| Supramolecule | Name: Human TOM-TIM22 supercomplex with substrate GGC1-sfGFP type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) / Strain: HEK293F / Organelle: mitochondria / Location in cell: mitochondria |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 3.6 mg/mL | ||||||||||||
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| Buffer | pH: 7.4 Component:
Details: 20 mM HEPES-NaOH pH 7.4, 100 mM NaCl, 0.06% digitonin | ||||||||||||
| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: OTHER | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV Details: 1.5 s blot time, 5 s wait time, 100% humidity, and 6 degree centigrade. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number real images: 31755 / Average exposure time: 5.44 sec. / 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 / Cs: 2.7 mm / 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 |
Movie
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation





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

