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Yorodumi- EMDB-4751: Yeast Vms1 (Q295L)-60S ribosomal subunit complex (pre-state with Arb1) -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-4751 | ||||||||||||
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Title | Yeast Vms1 (Q295L)-60S ribosomal subunit complex (pre-state with Arb1) | ||||||||||||
Map data | |||||||||||||
Sample |
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Function / homology | Function and homology information catalytic activity, acting on a tRNA / Cdc48p-Npl4p-Vms1p AAA ATPase complex / mitochondria-associated ubiquitin-dependent protein catabolic process / nuclear protein quality control by the ubiquitin-proteasome system / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / aminoacyl-tRNA hydrolase activity / maturation of 5.8S rRNA / hexon binding / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ...catalytic activity, acting on a tRNA / Cdc48p-Npl4p-Vms1p AAA ATPase complex / mitochondria-associated ubiquitin-dependent protein catabolic process / nuclear protein quality control by the ubiquitin-proteasome system / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / aminoacyl-tRNA hydrolase activity / maturation of 5.8S rRNA / hexon binding / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to cycloheximide / protein quality control for misfolded or incompletely synthesized proteins / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / ribosomal large subunit binding / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / negative regulation of mRNA splicing, via spliceosome / preribosome, large subunit precursor / L13a-mediated translational silencing of Ceruloplasmin expression / protein unfolding / translational elongation / ribosomal large subunit export from nucleus / 90S preribosome / regulation of translational fidelity / protein-RNA complex assembly / ribosomal subunit export from nucleus / ribosomal small subunit export from nucleus / translational termination / ERAD pathway / maturation of LSU-rRNA / RNA endonuclease activity / translation initiation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / rescue of stalled ribosome / assembly of large subunit precursor of preribosome / ribosomal large subunit biogenesis / cytosolic ribosome assembly / translational initiation / macroautophagy / maintenance of translational fidelity / modification-dependent protein catabolic process / protein tag activity / rRNA processing / ribosome biogenesis / viral capsid / 5S rRNA binding / large ribosomal subunit rRNA binding / ribosomal large subunit assembly / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytoplasmic translation / cytosolic large ribosomal subunit / Hydrolases; Acting on ester bonds / negative regulation of translation / rRNA binding / ribosome / protein ubiquitination / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / ubiquitin protein ligase binding / endoplasmic reticulum membrane / host cell nucleus / nucleolus / ATP hydrolysis activity / mitochondrion / RNA binding / ATP binding / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) / Baker's yeast (brewer's yeast) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||||||||
Authors | Su T / Izawa T / Cheng J / Yamashita Y / Berninghausen O / Inada T / Neupert W / Beckmann R | ||||||||||||
Funding support | Germany, 3 items
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Citation | Journal: Nature / Year: 2019 Title: Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis. Authors: Ting Su / Toshiaki Izawa / Matthias Thoms / Yui Yamashita / Jingdong Cheng / Otto Berninghausen / F Ulrich Hartl / Toshifumi Inada / Walter Neupert / Roland Beckmann / Abstract: Ribosome-associated quality control (RQC) provides a rescue pathway for eukaryotic cells to process faulty proteins after translational stalling of cytoplasmic ribosomes. After dissociation of ...Ribosome-associated quality control (RQC) provides a rescue pathway for eukaryotic cells to process faulty proteins after translational stalling of cytoplasmic ribosomes. After dissociation of ribosomes, the stalled tRNA-bound peptide remains associated with the 60S subunit and extended by Rqc2 by addition of C-terminal alanyl and threonyl residues (CAT tails), whereas Vms1 catalyses cleavage and release of the peptidyl-tRNA before or after addition of CAT tails. In doing so, Vms1 counteracts CAT-tailing of nuclear-encoded mitochondrial proteins that otherwise drive aggregation and compromise mitochondrial and cellular homeostasis. Here we present structural and functional insights into the interaction of Saccharomyces cerevisiae Vms1 with 60S subunits in pre- and post-peptidyl-tRNA cleavage states. Vms1 binds to 60S subunits with its Vms1-like release factor 1 (VLRF1), zinc finger and ankyrin domains. VLRF1 overlaps with the Rqc2 A-tRNA position and interacts with the ribosomal A-site, projecting its catalytic GSQ motif towards the CCA end of the tRNA, its Y285 residue dislodging the tRNA A73 for nucleolytic cleavage. Moreover, in the pre-state, we found the ABCF-type ATPase Arb1 in the ribosomal E-site, which stabilizes the delocalized A73 of the peptidyl-tRNA and stimulates Vms1-dependent tRNA cleavage. Our structural analysis provides mechanistic insights into the interplay of the RQC factors Vms1, Rqc2 and Arb1 and their role in the protection of mitochondria from the aggregation of toxic proteins. | ||||||||||||
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_4751.map.gz | 139 MB | EMDB map data format | |
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Header (meta data) | emd-4751-v30.xml emd-4751.xml | 66.1 KB 66.1 KB | Display Display | EMDB header |
Images | emd_4751.png | 168.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4751 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4751 | HTTPS FTP |
-Validation report
Summary document | emd_4751_validation.pdf.gz | 252.1 KB | Display | EMDB validaton report |
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Full document | emd_4751_full_validation.pdf.gz | 251.3 KB | Display | |
Data in XML | emd_4751_validation.xml.gz | 7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4751 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4751 | HTTPS FTP |
-Related structure data
Related structure data | 6r84MC 4752C 4753C 6r86C 6r87C 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_4751.map.gz / Format: CCP4 / Size: 236.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.084 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 : Vms1-60S ribosomal subunit complex
+Supramolecule #1: Vms1-60S ribosomal subunit complex
+Supramolecule #2: 60S ribosomal subunit
+Supramolecule #3: Vms1
+Macromolecule #1: ABC transporter ATP-binding protein ARB1
+Macromolecule #2: Protein VMS1,Vms1,Protein VMS1,Vms1
+Macromolecule #3: Eukaryotic translation initiation factor 6
+Macromolecule #4: 60S ribosomal protein L34-A
+Macromolecule #5: 60S ribosomal protein L7-A
+Macromolecule #6: 60S ribosomal protein L35-A
+Macromolecule #7: 60S ribosomal protein L8-A
+Macromolecule #8: 60S ribosomal protein L36-A
+Macromolecule #9: 60S ribosomal protein L9-A
+Macromolecule #10: 60S ribosomal protein L37-A
+Macromolecule #11: 60S ribosomal protein L11-B
+Macromolecule #12: 60S ribosomal protein L38
+Macromolecule #13: 60S ribosomal protein L13-A
+Macromolecule #14: 60S ribosomal protein L39
+Macromolecule #15: 60S ribosomal protein L14-A
+Macromolecule #16: Ubiquitin-60S ribosomal protein L40
+Macromolecule #17: 60S ribosomal protein L15-A
+Macromolecule #18: 60S ribosomal protein L16-A
+Macromolecule #19: 60S ribosomal protein L17-A
+Macromolecule #20: 60S ribosomal protein L18-A
+Macromolecule #21: 60S ribosomal protein L10
+Macromolecule #22: 60S ribosomal protein L19-A
+Macromolecule #23: 60S ribosomal protein L20-A
+Macromolecule #24: 60S ribosomal protein L21-A
+Macromolecule #25: 60S ribosomal protein L22-A
+Macromolecule #26: 60S ribosomal protein L12-A
+Macromolecule #27: 60S acidic ribosomal protein P0
+Macromolecule #28: 60S ribosomal protein L23-A
+Macromolecule #30: 60S ribosomal protein L24-A
+Macromolecule #32: 60S ribosomal protein L25
+Macromolecule #33: 60S ribosomal protein L26-A
+Macromolecule #35: 60S ribosomal protein L27-A
+Macromolecule #36: 60S ribosomal protein L42-A
+Macromolecule #37: 60S ribosomal protein L28
+Macromolecule #38: 60S ribosomal protein L43-A
+Macromolecule #39: 60S ribosomal protein L29
+Macromolecule #40: 60S ribosomal protein L2-A
+Macromolecule #41: 60S ribosomal protein L30
+Macromolecule #42: 60S ribosomal protein L3
+Macromolecule #43: 60S ribosomal protein L31-A
+Macromolecule #44: 60S ribosomal protein L4-A
+Macromolecule #45: 60S ribosomal protein L32
+Macromolecule #46: 60S ribosomal protein L5
+Macromolecule #47: 60S ribosomal protein L33-A
+Macromolecule #48: 60S ribosomal protein L6-A
+Macromolecule #49: 60S ribosomal protein L1-A
+Macromolecule #29: 5S rRNA
+Macromolecule #31: 5.8S rRNA
+Macromolecule #34: tRNA-Ala
+Macromolecule #50: 25S rRNA
+Macromolecule #51: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 2.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 31832 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |