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Yorodumi- EMDB-19944: cryoEM structure of the Drosophila melanogaster TOM core complex -
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Open data
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Basic information
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| Title | cryoEM structure of the Drosophila melanogaster TOM core complex | |||||||||
Map data | Map of the translocase of the outer mitochondrial membrane of Drosophila melanogaster. Main 3D volume. Sharpened map. | |||||||||
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Keywords | Complex / outer membrane / mitochondria / membrane protein / TOM / translocase | |||||||||
| Function / homology | Function and homology informationmitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / protein transmembrane transport / positive regulation of protein targeting to mitochondrion / protein targeting to mitochondrion / porin activity / pore complex / protein import into mitochondrial matrix / protein transmembrane transporter activity / monoatomic ion transport ...mitochondrial outer membrane translocase complex / protein insertion into mitochondrial outer membrane / protein transmembrane transport / positive regulation of protein targeting to mitochondrion / protein targeting to mitochondrion / porin activity / pore complex / protein import into mitochondrial matrix / protein transmembrane transporter activity / monoatomic ion transport / cellular response to hypoxia / mitochondrial outer membrane / mitochondrion Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.35 Å | |||||||||
Authors | Ornelas P / Kuehlbrandt W | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: IUCrJ / Year: 2025Title: Structure of an ex vivoDrosophila TOM complex determined by single-particle cryoEM. Authors: Agalya Periasamy / Pamela Ornelas / Thomas Bausewein / Naomi Mitchell / Jiamin Zhao / Leonie M Quinn / Werner Kuehlbrandt / Jacqueline M Gulbis / ![]() Abstract: Most mitochondrial precursor proteins are encoded in the cell nucleus and synthesized on cytoplasmic ribosomes. The translocase of the outer membrane (TOM) is the main protein-import pore of ...Most mitochondrial precursor proteins are encoded in the cell nucleus and synthesized on cytoplasmic ribosomes. The translocase of the outer membrane (TOM) is the main protein-import pore of mitochondria, recognizing nascent precursors of mitochondrially targeted proteins and transferring them across the outer membrane. A 3.3 Å resolution map and molecular model of a TOM complex from Drosophila melanogaster, obtained by single-particle electron cryomicroscopy, is presented. As the first reported structure of a transgenic protein expressed and purified ex vivo from Drosophila, the method provides impetus for parallel structural and genetic analyses of protein complexes linked to human pathology. The core TOM complex extracted from native membranes of the D. melanogaster retina contains transgenic Tom40 co-assembled with four endogenous TOM components: Tom22, Tom5, Tom6 and Tom7. The Drosophila TOM structure presented here shows that the human and Drosophila TOM are very similar, with small conformational changes at two subunit interfaces attributable to variation in lipid-binding residues. The new structure provides an opportunity to pinpoint general features that differentiate the TOM structures of higher and unicellular eukaryotes. While the quaternary fold of the assembly is retained, local nuances of structural elements implicated in precursor import are indicative of subtle evolutionary change. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_19944.map.gz | 167.9 MB | EMDB map data format | |
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| Header (meta data) | emd-19944-v30.xml emd-19944.xml | 20.1 KB 20.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_19944_fsc.xml | 11.9 KB | Display | FSC data file |
| Images | emd_19944.png | 115.4 KB | ||
| Filedesc metadata | emd-19944.cif.gz | 6.4 KB | ||
| Others | emd_19944_half_map_1.map.gz emd_19944_half_map_2.map.gz | 165.1 MB 165.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19944 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19944 | HTTPS FTP |
-Validation report
| Summary document | emd_19944_validation.pdf.gz | 1016.5 KB | Display | EMDB validaton report |
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| Full document | emd_19944_full_validation.pdf.gz | 1016 KB | Display | |
| Data in XML | emd_19944_validation.xml.gz | 20.1 KB | Display | |
| Data in CIF | emd_19944_validation.cif.gz | 25.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19944 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19944 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9etmMC 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_19944.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Map of the translocase of the outer mitochondrial membrane of Drosophila melanogaster. Main 3D volume. Sharpened map. | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.837 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Volume half map A
| File | emd_19944_half_map_1.map | ||||||||||||
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| Annotation | Volume half map A | ||||||||||||
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| Density Histograms |
-Half map: Volume half map B
| File | emd_19944_half_map_2.map | ||||||||||||
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| Annotation | Volume half map B | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Translocase of the outer mitochondrial membrane core complex of D...
| Entire | Name: Translocase of the outer mitochondrial membrane core complex of Drosophila melanogaster |
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| Components |
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-Supramolecule #1: Translocase of the outer mitochondrial membrane core complex of D...
| Supramolecule | Name: Translocase of the outer mitochondrial membrane core complex of Drosophila melanogaster type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Mitochondrial import receptor subunit TOM6
| Macromolecule | Name: Mitochondrial import receptor subunit TOM6 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 4.883772 KDa |
| Sequence | String: PLSIVRSIYN NEFQWMLVKS YGLFFLGVRL AKEFVGVELM PS UniProtKB: GEO13367p1 |
-Macromolecule #2: Mitochondrial import receptor subunit TOM5
| Macromolecule | Name: Mitochondrial import receptor subunit TOM5 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 4.308033 KDa |
| Sequence | String: SQPDPAEEQK RVAAEVRFNF ILFGAVIAAV RLAPIVLKH UniProtKB: RH17559p |
-Macromolecule #3: Mitochondrial import receptor subunit TOM7
| Macromolecule | Name: Mitochondrial import receptor subunit TOM7 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.138079 KDa |
| Sequence | String: DRLGFVVGVV QTGFHWGFVP LVLYLGFMKG AEPGMPPLNL FSLLWQ UniProtKB: Mitochondrial import receptor subunit TOM7 homolog |
-Macromolecule #4: Mitochondrial import receptor subunit TOM22
| Macromolecule | Name: Mitochondrial import receptor subunit TOM22 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 5.352121 KDa |
| Sequence | String: ATVKSVKGFY SFSCNASWIF FTSAVILFAP VIFETERAQM EELHKSQ UniProtKB: Mitochondrial import receptor subunit TOM22 homolog |
-Macromolecule #5: Mitochondrial import receptor subunit TOM40
| Macromolecule | Name: Mitochondrial import receptor subunit TOM40 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 31.382713 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: AALENPGTVE ELHKKCKDIQ AITFEGAKIM LNKGLSNHFQ VSHTINMSNV VPSGYRFGAT YVGTKEFSPT EAFPVLLGDI DPAGNLNAN VIHQFSARLR CKFASQIQES KVVASQLTTD YRGSDYTLSL TVANPSIFTN SGVVVGQYLQ SVTPALALGS E LAYQFGPN ...String: AALENPGTVE ELHKKCKDIQ AITFEGAKIM LNKGLSNHFQ VSHTINMSNV VPSGYRFGAT YVGTKEFSPT EAFPVLLGDI DPAGNLNAN VIHQFSARLR CKFASQIQES KVVASQLTTD YRGSDYTLSL TVANPSIFTN SGVVVGQYLQ SVTPALALGS E LAYQFGPN VPGRQIAIMS VVGRYTAGSS VWSGTLGQSG LHVCYYQKAS DQLQIGAEVE TSLRMQESVA TLAYQIDLPK AN LVFRGGI DSNWQIFGVL EKRLAPLPFT LALSGRMNHV KNNFRLGCGL MIG UniProtKB: Mitochondrial import receptor subunit TOM40 homolog 1 |
-Macromolecule #6: DIUNDECYL PHOSPHATIDYL CHOLINE
| Macromolecule | Name: DIUNDECYL PHOSPHATIDYL CHOLINE / type: ligand / ID: 6 / Number of copies: 5 / Formula: PLC |
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| Molecular weight | Theoretical: 622.834 Da |
| Chemical component information | ![]() ChemComp-PLC: |
-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: 7.4 |
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| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Detector mode: COUNTING / Average electron dose: 55.0 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: 2.4 µm / Nominal defocus min: 1.4000000000000001 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Germany, 1 items
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Processing
FIELD EMISSION GUN

