+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-2650 | |||||||||
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Title | Structure of the mammalian ribosome-Sec61 complex | |||||||||
Map data | Final map for mammalian ribosome in complex with Sec61 in idle configuration with the large subunit masked along refinement | |||||||||
Sample |
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Keywords | translation / ribosome / mammalian / sec61 | |||||||||
Function / homology | Function and homology information regulation of cell cycle => GO:0051726 / regulation of cell cycle => GO:0051726 / : / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Major pathway of rRNA processing in the nucleolus and cytosol / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) ...regulation of cell cycle => GO:0051726 / regulation of cell cycle => GO:0051726 / : / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Major pathway of rRNA processing in the nucleolus and cytosol / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / protein-transporting ATPase activity / translation at presynapse / embryonic brain development / alpha-beta T cell differentiation / cytoplasmic side of rough endoplasmic reticulum membrane / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / regulation of translation involved in cellular response to UV / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / organelle membrane / positive regulation of signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / protein localization to nucleus / protein targeting / protein-RNA complex assembly / cellular response to actinomycin D / negative regulation of ubiquitin-dependent protein catabolic process / membrane => GO:0016020 / translation regulator activity / rough endoplasmic reticulum / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / maturation of LSU-rRNA / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / innate immune response in mucosa / positive regulation of translation / cellular response to gamma radiation / mRNA 5'-UTR binding / transcription coactivator binding / cytoplasmic ribonucleoprotein granule / modification-dependent protein catabolic process / protein tag activity / rRNA processing / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit / protein transport / antibacterial humoral response / regulation of translation / presynapse / heparin binding / 5S rRNA binding / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / postsynaptic density / protein stabilization / rRNA binding / defense response to Gram-positive bacterium / ribosome / structural constituent of ribosome / protein ubiquitination / translation / ribonucleoprotein complex / mRNA binding / glutamatergic synapse / ubiquitin protein ligase binding / positive regulation of cell population proliferation / synapse / positive regulation of gene expression / nucleolus / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / RNA binding / extracellular space / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Sus scrofa domesticus (domestic pig) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Voorhees RM / Fernandez IS / Scheres SHW / Hegde R | |||||||||
Citation | Journal: Cell / Year: 2014 Title: Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution. Authors: Rebecca M Voorhees / Israel S Fernández / Sjors H W Scheres / Ramanujan S Hegde / Abstract: Cotranslational protein translocation is a universally conserved process for secretory and membrane protein biosynthesis. Nascent polypeptides emerging from a translating ribosome are either ...Cotranslational protein translocation is a universally conserved process for secretory and membrane protein biosynthesis. Nascent polypeptides emerging from a translating ribosome are either transported across or inserted into the membrane via the ribosome-bound Sec61 channel. Here, we report structures of a mammalian ribosome-Sec61 complex in both idle and translating states, determined to 3.4 and 3.9 Å resolution. The data sets permit building of a near-complete atomic model of the mammalian ribosome, visualization of A/P and P/E hybrid-state tRNAs, and analysis of a nascent polypeptide in the exit tunnel. Unprecedented chemical detail is observed for both the ribosome-Sec61 interaction and the conformational state of Sec61 upon ribosome binding. Comparison of the maps from idle and translating complexes suggests how conformational changes to the Sec61 channel could facilitate translocation of a secreted polypeptide. The high-resolution structure of the mammalian ribosome-Sec61 complex provides a valuable reference for future functional and structural studies. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_2650.map.gz | 31.1 MB | EMDB map data format | |
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Header (meta data) | emd-2650-v30.xml emd-2650.xml | 8.6 KB 8.6 KB | Display Display | EMDB header |
Images | EMD-2650.png | 307.4 KB | ||
Others | emd_2650_half_map_1.map.gz emd_2650_half_map_2.map.gz | 209.7 MB 209.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-2650 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-2650 | HTTPS FTP |
-Validation report
Summary document | emd_2650_validation.pdf.gz | 337.1 KB | Display | EMDB validaton report |
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Full document | emd_2650_full_validation.pdf.gz | 336.7 KB | Display | |
Data in XML | emd_2650_validation.xml.gz | 7.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-2650 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-2650 | HTTPS FTP |
-Related structure data
Related structure data | 3j7qMC 2644C 2646C 2649C 3j7oC 3j7pC 3j7rC M: atomic model generated by this map C: citing same article (ref.) |
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Similar 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_2650.map.gz / Format: CCP4 / Size: 276 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Final map for mammalian ribosome in complex with Sec61 in idle configuration with the large subunit masked along refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Supplemental map: emd 2650 half map 1.map
File | emd_2650_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: emd 2650 half map 2.map
File | emd_2650_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Mammalian ribosome in complex with Sec61 in a idle configuration ...
Entire | Name: Mammalian ribosome in complex with Sec61 in a idle configuration with the large subunit (60S) masked during processing. |
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Components |
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-Supramolecule #1000: Mammalian ribosome in complex with Sec61 in a idle configuration ...
Supramolecule | Name: Mammalian ribosome in complex with Sec61 in a idle configuration with the large subunit (60S) masked during processing. type: sample / ID: 1000 / Number unique components: 2 |
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-Supramolecule #1: Mammalian ribosome
Supramolecule | Name: Mammalian ribosome / type: complex / ID: 1 / Recombinant expression: No / Ribosome-details: ribosome-eukaryote: ALL |
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Source (natural) | Organism: Sus scrofa domesticus (domestic pig) / synonym: Domestic Pig / Tissue: pancreas |
-Macromolecule #1: Sec61
Macromolecule | Name: Sec61 / type: protein_or_peptide / ID: 1 / Recombinant expression: No |
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Source (natural) | Organism: Sus scrofa domesticus (domestic pig) / synonym: Domestic Pig |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 Details: 50mM HEPES, 200mM K-acetate, 15mM Mg-acetate, 1mM DTT |
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Grid | Details: Quantifoil R2/2 400 mesh copper grids. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 120 K / Instrument: FEI VITROBOT MARK IV Method: 3uL of sampled was incubated on the grid for 30 seconds before blotting for 9 second |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Date | Apr 7, 2014 |
Image recording | Category: CCD / Film or detector model: FEI FALCON II (4k x 4k) / Number real images: 1900 / Average electron dose: 25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 0.003 µm / Nominal defocus min: 0.001 µm / Nominal magnification: 47000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
CTF correction | Details: Each particle |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: OTHER / Software - Name: Relion / Number images used: 80019 |