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Yorodumi- PDB-7as9: Bacillus subtilis ribosome-associated quality control complex sta... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7as9 | ||||||||||||||||||
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Title | Bacillus subtilis ribosome-associated quality control complex state A. Ribosomal 50S subunit with peptidyl tRNA in the A/P position and RqcH. | ||||||||||||||||||
Components |
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Keywords | TRANSLATION / 50S / tRNA / RQC / RqcH / peptidyl-tRNA | ||||||||||||||||||
Function / homology | Function and homology information RQC complex / positive regulation of rRNA processing / nucleoid / ribosomal large subunit binding / rescue of stalled ribosome / rRNA processing / large ribosomal subunit / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity ...RQC complex / positive regulation of rRNA processing / nucleoid / ribosomal large subunit binding / rescue of stalled ribosome / rRNA processing / large ribosomal subunit / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / DNA binding / RNA binding / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | Bacillus subtilis (bacteria) Bacillus subtilis subsp. subtilis str. 168 (bacteria) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||||||||
Authors | Crowe-McAuliffe, C. / Wilson, D.N. | ||||||||||||||||||
Funding support | Germany, Sweden, 5items
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Citation | Journal: Mol Cell / Year: 2021 Title: Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP. Authors: Caillan Crowe-McAuliffe / Hiraku Takada / Victoriia Murina / Christine Polte / Sergo Kasvandik / Tanel Tenson / Zoya Ignatova / Gemma C Atkinson / Daniel N Wilson / Vasili Hauryliuk / Abstract: In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, ...In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit. | ||||||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7as9.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7as9.ent.gz | 1.6 MB | Display | PDB format |
PDBx/mmJSON format | 7as9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7as9_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 7as9_full_validation.pdf.gz | 1.8 MB | Display | |
Data in XML | 7as9_validation.xml.gz | 145.1 KB | Display | |
Data in CIF | 7as9_validation.cif.gz | 253.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/7as9 ftp://data.pdbj.org/pub/pdb/validation_reports/as/7as9 | HTTPS FTP |
-Related structure data
Related structure data | 11890MC 7as8C 7asaC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | |
EM raw data | EMPIAR-10540 (Title: Affinity-purified RqcH-ribosome-associated quality control complexes from Bacillus subtilis Data size: 514.6 Data #1: Unaligned multi-frame micrographs of affinity-purified RqcH ribosome-associated quality control complexes from Bacillus subtilis [micrographs - multiframe]) |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 1 types, 1 molecules 0
#1: Protein | Mass: 68341.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (strain 168) (bacteria) Strain: 168 / Gene: rqcH, yloA, BSU15640 / Production host: Bacillus subtilis (strain 168) (bacteria) / References: UniProt: O34693 |
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-RNA chain , 3 types, 3 molecules 2AB
#2: RNA chain | Mass: 24491.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Bacillus subtilis subsp. subtilis str. 168 (bacteria) |
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#3: RNA chain | Mass: 949010.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Bacillus subtilis subsp. subtilis str. 168 (bacteria) |
#4: RNA chain | Mass: 38423.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Bacillus subtilis subsp. subtilis str. 168 (bacteria) |
+50S ribosomal protein ... , 28 types, 28 molecules EFGHIKLNOPQRSTUVWXYabcdfghij
-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component |
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Molecular weight | Value: 1.6 MDa / Experimental value: NO | ||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) | Organism: Bacillus subtilis (strain 168) (bacteria) | ||||||||||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 29 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 2 |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 10703 / Symmetry type: POINT |