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Yorodumi- PDB-8oj8: 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8oj8 | ||||||||||||||||||
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| Title | 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) | ||||||||||||||||||
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Keywords | RIBOSOME / ER / UFMylation / recycling | ||||||||||||||||||
| Function / homology | Function and homology informationUFM1 ligase activity / positive regulation of reticulophagy / UFM1 transferase activity / protein K69-linked ufmylation / protein ufmylation / : / endoplasmic reticulum Sec complex / pronephric nephron development / negative regulation of IRE1-mediated unfolded protein response / cotranslational protein targeting to membrane ...UFM1 ligase activity / positive regulation of reticulophagy / UFM1 transferase activity / protein K69-linked ufmylation / protein ufmylation / : / endoplasmic reticulum Sec complex / 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 / regulation of intracellular estrogen receptor signaling pathway / regulation of proteasomal ubiquitin-dependent protein catabolic process / protein insertion into ER membrane / regulation of megakaryocyte differentiation / regulation of fatty acid biosynthetic process / miRNA-mediated post-transcriptional gene silencing / protein targeting to ER / post-translational protein targeting to membrane, translocation / negative regulation of T cell mediated immune response to tumor cell / SRP-dependent cotranslational protein targeting to membrane, translocation / miRNA-mediated gene silencing by inhibition of translation / signal sequence receptor activity / translation at presynapse / response to insecticide / Transferases; Acyltransferases; Aminoacyltransferases / regulation of translation involved in cellular response to UV / eukaryotic 80S initiation complex / ribosome disassembly / ribosomal protein import into nucleus / regulation of G1 to G0 transition / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / regulation of reactive oxygen species metabolic process / regulation of canonical NF-kappaB signal transduction / reticulophagy / protein-DNA complex disassembly / regulation of glycolytic process / epidermal growth factor binding / negative regulation of formation of translation preinitiation complex / positive regulation of DNA damage response, signal transduction by p53 class mediator / GAIT complex / maturation of 5.8S rRNA / TORC2 complex binding / G1 to G0 transition / PD-L1(CD274) glycosylation and translocation to plasma membrane / Enterobacterial factors antagonize host defense / retrograde protein transport, ER to cytosol / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of T cell activation / cytoplasmic side of rough endoplasmic reticulum membrane / hematopoietic stem cell differentiation / negative regulation of myoblast fusion / ribosomal large subunit binding / male meiosis I / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / Dengue Virus Genome Translation and Replication / Maturation of DENV proteins / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / Protein hydroxylation / transmembrane protein transporter activity / Peptide chain elongation / protein targeting / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / protein localization to nucleus / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274) / negative regulation of ubiquitin-dependent protein catabolic process / ubiquitin ligase inhibitor activity / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / positive regulation of signal transduction by p53 class mediator / ribosomal subunit export from nucleus / GTP hydrolysis and joining of the 60S ribosomal subunit / embryo implantation / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / GSK3B-mediated proteasomal degradation of PD-L1(CD274) / SPOP-mediated proteasomal degradation of PD-L1(CD274) / maturation of LSU-rRNA / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / protein-RNA complex assembly / ERAD pathway / rough endoplasmic reticulum / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / negative regulation of protein ubiquitination / translation initiation factor activity / mRNA Polyadenylation / rescue of stalled cytosolic ribosome / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / DNA damage checkpoint signaling / Maturation of protein E / MDM2/MDM4 family protein binding / Maturation of protein E / ER Quality Control Compartment (ERQC) Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||
| 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 | 8oj8.cif.gz | 3.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8oj8.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8oj8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/8oj8 ftp://data.pdbj.org/pub/pdb/validation_reports/oj/8oj8 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 16908MC ![]() 8ohdC ![]() 8oj0C ![]() 8oj5C C: citing same article ( M: map data used to model this data |
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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: 52295.379 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 , 4 types, 4 molecules AKLILm
| #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: 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: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 20750 / Symmetry type: POINT |
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About Yorodumi



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







PDBj




















































FIELD EMISSION GUN