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Yorodumi- EMDB-1169: ERj1p uses a universal ribosomal adaptor site to coordinate the 8... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1169 | |||||||||
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Title | ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane. | |||||||||
Map data | Volume of canine 80S+ErjC-dC | |||||||||
Sample |
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Biological species | Canis lupus familiaris (dog) / Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 20.0 Å | |||||||||
Authors | Blau M / Mullapudi S / Becker T / Dudek J / Zimmermann R / Penczek PA / Beckmann R | |||||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2005 Title: ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane. Authors: Michael Blau / Srinivas Mullapudi / Thomas Becker / Johanna Dudek / Richard Zimmermann / Pawel A Penczek / Roland Beckmann / Abstract: Ribosomes translating secretory and membrane proteins are targeted to the endoplasmic reticulum membrane and attach to the protein-conducting channel and ribosome-associated membrane proteins (RAMPs). ...Ribosomes translating secretory and membrane proteins are targeted to the endoplasmic reticulum membrane and attach to the protein-conducting channel and ribosome-associated membrane proteins (RAMPs). Recently, a new RAMP, ERj1p, has been identified that recruits BiP to ribosomes and regulates translational activity. Here we present the cryo-EM structure of a ribosome-ERj1p complex, revealing how ERj1p coordinates the ribosome at the membrane and how allosteric effects may mediate ERj1p's regulatory activity. | |||||||||
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_1169.map.gz | 10 MB | EMDB map data format | |
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Header (meta data) | emd-1169-v30.xml emd-1169.xml | 6.7 KB 6.7 KB | Display Display | EMDB header |
Images | 1169.gif | 43.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1169 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1169 | 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_1169.map.gz / Format: CCP4 / Size: 11.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Volume of canine 80S+ErjC-dC | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 3.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : canine ribosome with bound ERj
Entire | Name: canine ribosome with bound ERj |
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Components |
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-Supramolecule #1000: canine ribosome with bound ERj
Supramolecule | Name: canine ribosome with bound ERj / type: sample / ID: 1000 / Number unique components: 2 |
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-Supramolecule #1: canine ribosome
Supramolecule | Name: canine ribosome / type: complex / ID: 1 / Name.synonym: ribosome / Recombinant expression: No / Ribosome-details: ribosome-eukaryote: ALL |
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Source (natural) | Organism: Canis lupus familiaris (dog) / synonym: Dog |
-Macromolecule #1: ERjIp
Macromolecule | Name: ERjIp / type: protein_or_peptide / ID: 1 / Name.synonym: ERjC-dC / Recombinant expression: Yes |
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Source (natural) | Organism: Mus musculus (house mouse) / synonym: House mouse |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Vitrification | Cryogen name: ETHANE |
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-Electron microscopy
Microscope | JEOL KYOTO-3000SFF |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Sample stage | Specimen holder: Gathan / Specimen holder model: GATAN LIQUID NITROGEN |
-Image processing
Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 20.0 Å |
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