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Yorodumi- PDB-8oj0: 60S ribosomal subunit bound to the E3-UFM1 complex - state 2 (native) -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8oj0 | ||||||||||||||||||
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| Title | 60S ribosomal subunit bound to the E3-UFM1 complex - state 2 (native) | ||||||||||||||||||
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Keywords | RIBOSOME / UFMylation / ER / Recycling | ||||||||||||||||||
| Function / homology | Function and homology informationpositive regulation of I-kappaB phosphorylation / UFM1 ligase activity / UFM1-modified protein reader activity / positive regulation of reticulophagy / regulation of phosphatase activity / apoptotic nuclear changes / definitive erythrocyte differentiation / UFM1 transferase activity / negative regulation of protein serine/threonine kinase activity / positive regulation of protein localization to endoplasmic reticulum ...positive regulation of I-kappaB phosphorylation / UFM1 ligase activity / UFM1-modified protein reader activity / positive regulation of reticulophagy / regulation of phosphatase activity / apoptotic nuclear changes / definitive erythrocyte differentiation / UFM1 transferase activity / negative regulation of protein serine/threonine kinase activity / positive regulation of protein localization to endoplasmic reticulum / protein K69-linked ufmylation / negative regulation of protein kinase activity by regulation of protein phosphorylation / protein ufmylation / : / endoplasmic reticulum Sec complex / positive regulation of plasma cell differentiation / pronephric nephron development / negative regulation of IRE1-mediated unfolded protein response / cotranslational protein targeting to membrane / endoplasmic reticulum quality control compartment / Ssh1 translocon complex / Sec61 translocon complex / lamin filament / protein insertion into ER membrane / regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of megakaryocyte differentiation / regulation of fatty acid biosynthetic process / positive regulation of cell cycle G1/S phase transition / protein localization to endoplasmic reticulum / miRNA-mediated post-transcriptional gene silencing / protein targeting to ER / SRP-dependent cotranslational protein targeting to membrane, translocation / negative regulation of T cell mediated immune response to tumor cell / regulation of intracellular estrogen receptor signaling pathway / miRNA-mediated gene silencing by inhibition of translation / signal sequence receptor activity / translation at presynapse / mitotic G2/M transition checkpoint / post-translational protein targeting to membrane, translocation / regulation of cyclin-dependent protein serine/threonine kinase activity / exit from mitosis / optic nerve development / response to insecticide / regulation of translation involved in cellular response to UV / cartilage development / Transferases; Acyltransferases; Aminoacyltransferases / eukaryotic 80S initiation complex / positive regulation of proteasomal protein catabolic process / ribosomal protein import into nucleus / negative regulation of formation of translation preinitiation complex / mitogen-activated protein kinase binding / regulation of canonical NF-kappaB signal transduction / axial mesoderm development / ribosome disassembly / regulation of G1 to G0 transition / retinal ganglion cell axon guidance / protein-DNA complex disassembly / response to L-glutamate / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / reticulophagy / : / 90S preribosome assembly / regulation of glycolytic process / regulation of neuron differentiation / alpha-beta T cell differentiation / positive regulation of DNA damage response, signal transduction by p53 class mediator / epidermal growth factor binding / GAIT complex / regulation of reactive oxygen species metabolic process / TORC2 complex binding / maturation of 5.8S rRNA / negative regulation of protein import into nucleus / negative regulation of MAP kinase activity / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / G1 to G0 transition / retrograde protein transport, ER to cytosol / middle ear morphogenesis / negative regulation of T cell activation / cytoplasmic side of rough endoplasmic reticulum membrane / negative regulation of PERK-mediated unfolded protein response / negative regulation of protein phosphorylation / mitotic G2 DNA damage checkpoint signaling / ribosomal large subunit binding / homeostatic process / macrophage chemotaxis / lung morphogenesis / positive regulation of natural killer cell proliferation / male meiosis I / Protein hydroxylation / ubiquitin-like protein ligase binding / transmembrane protein transporter activity / Peptide chain elongation / RHOA GTPase cycle / positive regulation of glial cell proliferation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / hematopoietic stem cell differentiation / blastocyst development / SRP-dependent cotranslational protein targeting to membrane Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) Homo sapiens environmental sample (environmental samples) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||
Authors | Penchev, I. / DaRosa, P.A. / Becker, T. / Beckmann, R. / Kopito, R. | ||||||||||||||||||
| Funding support | European Union, Germany, United Kingdom, United States, 5items
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Citation | Journal: Nature / Year: 2024Title: UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER. Authors: Paul A DaRosa / Ivan Penchev / Samantha C Gumbin / Francesco Scavone / Magda Wąchalska / Joao A Paulo / Alban Ordureau / Joshua J Peter / Yogesh Kulathu / J Wade Harper / Thomas Becker / ...Authors: Paul A DaRosa / Ivan Penchev / Samantha C Gumbin / Francesco Scavone / Magda Wąchalska / Joao A Paulo / Alban Ordureau / Joshua J Peter / Yogesh Kulathu / J Wade Harper / Thomas Becker / Roland Beckmann / Ron R Kopito / ![]() Abstract: Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is widely used by eukaryotic cells to control protein fate and cell behaviour. UFM1 is a UBL that ...Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is widely used by eukaryotic cells to control protein fate and cell behaviour. UFM1 is a UBL that predominantly modifies a single lysine residue on a single ribosomal protein, uL24 (also called RPL26), on ribosomes at the cytoplasmic surface of the endoplasmic reticulum (ER). UFM1 conjugation (UFMylation) facilitates the rescue of 60S ribosomal subunits (60S) that are released after ribosome-associated quality-control-mediated splitting of ribosomes that stall during co-translational translocation of secretory proteins into the ER. Neither the molecular mechanism by which the UFMylation machinery achieves such precise target selection nor how this ribosomal modification promotes 60S rescue is known. Here we show that ribosome UFMylation in vivo occurs on free 60S and we present sequential cryo-electron microscopy snapshots of the heterotrimeric UFM1 E3 ligase (E3(UFM1)) engaging its substrate uL24. E3(UFM1) binds the L1 stalk, empty transfer RNA-binding sites and the peptidyl transferase centre through carboxy-terminal domains of UFL1, which results in uL24 modification more than 150 Å away. After catalysing UFM1 transfer, E3(UFM1) remains stably bound to its product, UFMylated 60S, forming a C-shaped clamp that extends all the way around the 60S from the transfer RNA-binding sites to the polypeptide tunnel exit. Our structural and biochemical analyses suggest a role for E3(UFM1) in post-termination release and recycling of the large ribosomal subunit from the ER membrane. | ||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8oj0.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8oj0.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8oj0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/8oj0 ftp://data.pdbj.org/pub/pdb/validation_reports/oj/8oj0 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 16902MC ![]() 8ohdC ![]() 8oj5C ![]() 8oj8C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein transport protein Sec61 subunit ... , 3 types, 3 molecules 123
| #1: Protein | Mass: 52279.379 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P38377 |
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| #2: Protein | Mass: 7752.325 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60059 |
| #3: Protein | Mass: 9987.456 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60468 |
-RNA chain , 3 types, 3 molecules 578
| #4: RNA chain | Mass: 1640166.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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| #5: RNA chain | Mass: 38998.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 23898 |
| #6: RNA chain | Mass: 50449.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 555853 |
-Protein , 7 types, 7 molecules ABCDKLILm
| #7: Protein | Mass: 89722.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UFL1, KIAA0776, MAXER, NLBP, RCAD / Production host: Homo sapiens (human)References: UniProt: O94874, Transferases; Acyltransferases; Aminoacyltransferases |
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| #8: Protein | Mass: 56977.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96JB5 |
| #9: Protein | Mass: 35663.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96HY6 |
| #10: Protein | Mass: 9128.552 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61960 |
| #11: Protein | Mass: 26620.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56537 |
| #20: Protein | Mass: 24552.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96L21 |
| #49: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62987 |
+60S ribosomal protein ... , 40 types, 40 molecules LALBLCLDLELFLGLHLJLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLeLf...
-Non-polymers , 2 types, 225 molecules 


| #54: Chemical | ChemComp-MG / #55: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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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 |
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Sample preparation
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| Source (natural) |
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| Source (recombinant) | Organism: Homo sapiens (human) | ||||||||||||||||||||||||
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 60 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: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 20377 / Symmetry type: POINT |
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About Yorodumi



Homo sapiens (human)
Germany,
United Kingdom,
United States, 5items
Citation








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FIELD EMISSION GUN