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- PDB-9gy4: 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC mach... -
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Basic information
Entry | Database: PDB / ID: 9gy4 | ||||||||||||
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Title | 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (Composite map) | ||||||||||||
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![]() | RIBOSOME / 60S / UFMylation / ER / RQC | ||||||||||||
Function / homology | ![]() positive regulation of metallopeptidase activity / : / positive regulation of I-kappaB phosphorylation / alpha-aminoacyl-tRNA binding / UFM1 ligase activity / UFM1-modified protein reader activity / positive regulation of reticulophagy / regulation of phosphatase activity / apoptotic nuclear changes / definitive erythrocyte differentiation ...positive regulation of metallopeptidase activity / : / positive regulation of I-kappaB phosphorylation / alpha-aminoacyl-tRNA binding / UFM1 ligase activity / UFM1-modified protein reader activity / positive regulation of reticulophagy / regulation of phosphatase activity / apoptotic nuclear changes / definitive erythrocyte differentiation / CAT tailing / UFM1 transferase activity / positive regulation of protein localization to endoplasmic reticulum / protein K69-linked ufmylation / positive regulation of proteolysis involved in protein catabolic process / negative regulation of protein kinase activity by regulation of protein phosphorylation / protein ufmylation / positive regulation of plasma cell differentiation / negative regulation of protein serine/threonine kinase activity / RQC complex / negative regulation of IRE1-mediated unfolded protein response / regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of T cell mediated immune response to tumor cell / protein localization to endoplasmic reticulum / positive regulation of cell cycle G1/S phase transition / negative regulation of T cell activation / regulation of intracellular estrogen receptor signaling pathway / eukaryotic 80S initiation complex / negative regulation of protein neddylation / positive regulation of proteasomal protein catabolic process / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / axial mesoderm development / mitotic G2/M transition checkpoint / ribosomal protein import into nucleus / 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 / 90S preribosome assembly / nuclear export / ribosome disassembly / Transferases; Acyltransferases; Aminoacyltransferases / regulation of canonical NF-kappaB signal transduction / GAIT complex / mitogen-activated protein kinase binding / A band / positive regulation of DNA damage response, signal transduction by p53 class mediator / TORC2 complex binding / alpha-beta T cell differentiation / reticulophagy / G1 to G0 transition / regulation of cyclin-dependent protein serine/threonine kinase activity / ribosome-associated ubiquitin-dependent protein catabolic process / cartilage development / regulation of neuron differentiation / middle ear morphogenesis / exit from mitosis / translation at presynapse / optic nerve development / cytoplasmic side of rough endoplasmic reticulum membrane / retinal ganglion cell axon guidance / negative regulation of protein import into nucleus / negative regulation of ubiquitin protein ligase activity / response to L-glutamate / homeostatic process / response to aldosterone / negative regulation of NF-kappaB transcription factor activity / macrophage chemotaxis / mitotic G2 DNA damage checkpoint signaling / negative regulation of PERK-mediated unfolded protein response / lung morphogenesis / male meiosis I / ribosomal large subunit binding / Protein hydroxylation / ubiquitin-like protein ligase binding / Peptide chain elongation / Selenocysteine synthesis / negative regulation of protein phosphorylation / positive regulation of signal transduction by p53 class mediator / Formation of a pool of free 40S subunits / ubiquitin ligase inhibitor activity / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / blastocyst development / cellular response to actinomycin D / negative regulation of ubiquitin-dependent protein catabolic process / Viral mRNA Translation / RHOA GTPase cycle / negative regulation of MAP kinase activity / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / protein localization to nucleus / hematopoietic stem cell differentiation / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / NF-kappaB binding / ubiquitin-like ligase-substrate adaptor activity / Major pathway of rRNA processing in the nucleolus and cytosol / protein targeting / protein-RNA complex assembly Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||||||||
![]() | Penchev, I. / Gumbin, S. / Becker, T. / Kopito, R. / Beckmann, R. | ||||||||||||
Funding support | European Union, ![]() ![]()
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![]() | ![]() Title: UFMylation orchestrates spatiotemporal coordination of RQC at the ER. Authors: Ivan Penchev / Samantha Gumbin / Francesco Scavone / Otto Berninghausen / Thomas Becker / Ron Kopito / Roland Beckmann / ![]() ![]() Abstract: Degradation of arrest peptides from endoplasmic reticulum (ER) translocon-bound 60 ribosomal subunits via the ribosome-associated quality control (ER-RQC) pathway requires covalent modification of ...Degradation of arrest peptides from endoplasmic reticulum (ER) translocon-bound 60 ribosomal subunits via the ribosome-associated quality control (ER-RQC) pathway requires covalent modification of RPL26/uL24 on 60 ribosomal subunits with UFM1. However, the underlying mechanism that coordinates the UFMylation and RQC pathways remains elusive. Structural analysis of ER-RQC intermediates revealed concomitant binding and direct interaction of the UFMylation and RQC machineries on the 60. In the presence of an arrested peptidyl-transfer RNA, the RQC factor NEMF and the UFM1 E3 ligase (E3) form a direct interaction via the UFL1 subunit of E3, and UFL1 adopts a conformation distinct from that previously observed for posttermination 60. While this concomitant binding occurs on translocon-bound 60, LTN1 recruitment and arrest peptide degradation require UFMylation-dependent 60 dissociation from the translocon. These data reveal a mechanism by which the UFMylation cycle orchestrates ER-RQC. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 51681MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-RNA chain , 4 types, 4 molecules 578G
#1: RNA chain | Mass: 1640166.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: RNA chain | Mass: 38998.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: RNA chain | Mass: 50449.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#9: RNA chain | Mass: 24502.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 9 types, 9 molecules BCDEFLILmZs
#4: Protein | Mass: 56977.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#5: Protein | Mass: 35663.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#6: Protein | Mass: 9128.552 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#7: Protein | Mass: 89722.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: O94874, Transferases; Acyltransferases; Aminoacyltransferases |
#8: Protein | Mass: 200778.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: O94822, RING-type E3 ubiquitin transferase |
#17: Protein | Mass: 24552.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#46: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#51: Protein | Mass: 123146.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#53: Protein | Mass: 34309.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 38 types, 38 molecules LBLCLDLGLHLJLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLeLfLgLhLi...
-Large ribosomal subunit protein ... , 3 types, 3 molecules LELFt
#13: Protein | Mass: 32810.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#14: Protein | Mass: 29290.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#54: Protein | Mass: 17847.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 1 types, 1 molecules A
#55: Protein/peptide | Mass: 613.749 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 224 molecules 


#56: Chemical | ChemComp-MG / #57: Chemical | ChemComp-ZN / |
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-Details
Has ligand of interest | N |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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Molecular weight |
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Source (natural) |
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Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8461 / Symmetry type: POINT |