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Yorodumi- EMDB-1615: Three-dimensional structure of YidC bound to the translating ribosome -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1615 | |||||||||
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Title | Three-dimensional structure of YidC bound to the translating ribosome | |||||||||
Map data | This map shows YidC bound to the tunnel exit region of an ribosome nascent chain complex | |||||||||
Sample |
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Keywords | membrane protein insertion / ribosome / translation | |||||||||
Function / homology | : / protein insertion into membrane Function and homology information | |||||||||
Biological species | Escherichia coli (E. coli) / Escherichia coli K-12 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 14.4 Å | |||||||||
Authors | Kohler R / Boehringer D / Greber B / Bingel-Erlenmeyer R / Collinson I / Schaffitzel C / Ban N | |||||||||
Citation | Journal: Mol Cell / Year: 2009 Title: YidC and Oxa1 form dimeric insertion pores on the translating ribosome. Authors: Rebecca Kohler / Daniel Boehringer / Basil Greber / Rouven Bingel-Erlenmeyer / Ian Collinson / Christiane Schaffitzel / Nenad Ban / Abstract: The YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we present the structures of both ...The YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we present the structures of both Escherichia coli YidC and Saccharomyces cerevisiae Oxa1 bound to E. coli ribosome nascent chain complexes determined by cryo-electron microscopy. Dimers of YidC and Oxa1 are localized above the exit of the ribosomal tunnel. Crosslinking experiments show that the ribosome specifically stabilizes the dimeric state. Functionally important and conserved transmembrane helices of YidC and Oxa1 were localized at the dimer interface by cysteine crosslinking. Both Oxa1 and YidC dimers contact the ribosome at ribosomal protein L23 and conserved rRNA helices 59 and 24, similarly to what was observed for the nonhomologous SecYEG translocon. We suggest that dimers of the YidC and Oxa1 proteins form insertion pores and share a common overall architecture with the SecY monomer. | |||||||||
History |
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-Structure visualization
Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
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Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1615.map.gz | 4.5 MB | EMDB map data format | |
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Header (meta data) | emd-1615-v30.xml emd-1615.xml | 9.4 KB 9.4 KB | Display Display | EMDB header |
Images | 1615_1615.png | 175.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1615 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1615 | HTTPS FTP |
-Validation report
Summary document | emd_1615_validation.pdf.gz | 241.3 KB | Display | EMDB validaton report |
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Full document | emd_1615_full_validation.pdf.gz | 240.4 KB | Display | |
Data in XML | emd_1615_validation.xml.gz | 5.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1615 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1615 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_1615.map.gz / Format: CCP4 / Size: 4.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | This map shows YidC bound to the tunnel exit region of an ribosome nascent chain complex | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 3.76 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : YidC bound to a translating ribosome
Entire | Name: YidC bound to a translating ribosome |
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Components |
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-Supramolecule #1000: YidC bound to a translating ribosome
Supramolecule | Name: YidC bound to a translating ribosome / type: sample / ID: 1000 / Number unique components: 2 |
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Molecular weight | Experimental: 2.6 MDa / Theoretical: 2.6 MDa |
-Supramolecule #1: Ribosome nascent chain complex
Supramolecule | Name: Ribosome nascent chain complex / type: complex / ID: 1 / Name.synonym: Translating ribosome / Recombinant expression: No / Ribosome-details: ribosome-prokaryote: ALL |
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Source (natural) | Organism: Escherichia coli (E. coli) |
Molecular weight | Experimental: 2.6 MDa / Theoretical: 2.6 MDa |
-Macromolecule #1: YidC
Macromolecule | Name: YidC / type: protein_or_peptide / ID: 1 / Name.synonym: Membrane protein insertase / Number of copies: 2 / Oligomeric state: Dimer / Recombinant expression: Yes |
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Source (natural) | Organism: Escherichia coli K-12 (bacteria) / Location in cell: Membrane |
Molecular weight | Experimental: 62 KDa / Theoretical: 62 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) / Recombinant plasmid: peT24a |
Sequence | GO: protein insertion into membrane / InterPro: INTERPRO: IPR013308 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Grid | Details: 200 mesh copper |
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Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER / Details: Vitrification instrument: Plunger |
-Electron microscopy
Microscope | FEI TECNAI 20 |
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Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: NIKON SUPER COOLSCAN 9000 / Digitization - Sampling interval: 12.7 µm / Average electron dose: 15 e/Å2 / Bits/pixel: 16 |
Tilt angle min | 0 |
Tilt angle max | 0 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 50000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 50000 |
Sample stage | Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN |
-Image processing
CTF correction | Details: Each image |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 14.4 Å / Resolution method: OTHER / Software - Name: Imagic-5 Spider / Number images used: 24395 |