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Yorodumi- PDB-8ohd: 60S ribosomal subunit bound to the E3-UFM1 complex - state 3 (native) -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8ohd | ||||||||||||||||||
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| Title | 60S ribosomal subunit bound to the E3-UFM1 complex - state 3 (native) | ||||||||||||||||||
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Keywords | RIBOSOME / 60S / 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 / : / positive regulation of plasma cell differentiation / negative regulation of IRE1-mediated unfolded protein response / lamin filament / 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 / 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 / translation at presynapse / mitotic G2/M transition checkpoint / 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 / negative regulation of formation of translation preinitiation complex / positive regulation of proteasomal protein catabolic process / axial mesoderm development / ribosomal protein import into nucleus / regulation of G1 to G0 transition / mitogen-activated protein kinase binding / retinal ganglion cell axon guidance / regulation of canonical NF-kappaB signal transduction / ribosome disassembly / 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 neuron differentiation / : / alpha-beta T cell differentiation / regulation of glycolytic process / positive regulation of DNA damage response, signal transduction by p53 class mediator / GAIT complex / TORC2 complex binding / regulation of reactive oxygen species metabolic process / maturation of 5.8S rRNA / negative regulation of protein import into nucleus / negative regulation of MAP kinase activity / G1 to G0 transition / 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 / positive regulation of glial cell proliferation / RHOA GTPase cycle / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / hematopoietic stem cell differentiation / Eukaryotic Translation Termination / blastocyst development / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / positive regulation of signal transduction by p53 class mediator / protein localization to nucleus / negative regulation of ubiquitin-dependent protein catabolic process / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / NF-kappaB binding / GTP hydrolysis and joining of the 60S ribosomal subunit / ribosomal subunit export from nucleus / L13a-mediated translational silencing of Ceruloplasmin expression / protein targeting / Major pathway of rRNA processing in the nucleolus and cytosol / ubiquitin-like ligase-substrate adaptor activity / protein-RNA complex assembly Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 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 | 8ohd.cif.gz | 3.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ohd.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8ohd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oh/8ohd ftp://data.pdbj.org/pub/pdb/validation_reports/oh/8ohd | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 16880MC ![]() 8oj0C ![]() 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
-RNA chain , 3 types, 3 molecules 578
| #1: 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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| #2: 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 |
| #3: 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
| #4: 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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| #5: Protein | Mass: 56977.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96JB5 |
| #6: Protein | Mass: 35663.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96HY6 |
| #7: Protein | Mass: 9128.552 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61960 |
| #8: Protein | Mass: 26620.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56537 |
| #17: Protein | Mass: 24552.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96L21 |
| #46: 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 


| #51: Chemical | ChemComp-MG / #52: 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: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 123096 / Symmetry type: POINT |
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About Yorodumi



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







PDBj


















































FIELD EMISSION GUN