[English] 日本語
Yorodumi- PDB-8oj8: 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 8oj8 | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) | ||||||||||||||||||
Components |
| ||||||||||||||||||
Keywords | RIBOSOME / ER / UFMylation / recycling | ||||||||||||||||||
| Function / homology | Function and homology informationUFM1 ligase activity / positive regulation of reticulophagy / UFM1 transferase activity / positive regulation of proteolysis involved in protein catabolic process / 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 / positive regulation of proteolysis involved in protein catabolic process / 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 / regulation of proteasomal ubiquitin-dependent protein catabolic process / Sec61 translocon complex / lamin filament / regulation of fatty acid biosynthetic process / protein targeting to ER / protein insertion into ER membrane / regulation of megakaryocyte differentiation / negative regulation of T cell mediated immune response to tumor cell / negative regulation of T cell activation / miRNA-mediated post-transcriptional gene silencing / SRP-dependent cotranslational protein targeting to membrane, translocation / regulation of intracellular estrogen receptor signaling pathway / miRNA-mediated gene silencing by inhibition of translation / translation at presynapse / signal sequence binding / exit from mitosis / eukaryotic 80S initiation complex / negative regulation of protein neddylation / optic nerve development / response to insecticide / regulation of translation involved in cellular response to UV / axial mesoderm development / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / post-translational protein targeting to membrane, translocation / ribosomal protein import into nucleus / protein-DNA complex disassembly / 90S preribosome assembly / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / retinal ganglion cell axon guidance / Transferases; Acyltransferases; Aminoacyltransferases / ribosome disassembly / response to L-glutamate / regulation of canonical NF-kappaB signal transduction / GAIT complex / positive regulation of DNA damage response, signal transduction by p53 class mediator / TORC2 complex binding / alpha-beta T cell differentiation / G1 to G0 transition / reticulophagy / regulation of glycolytic process / middle ear morphogenesis / regulation of reactive oxygen species metabolic process / epidermal growth factor binding / cytoplasmic side of rough endoplasmic reticulum membrane / retrograde protein transport, ER to cytosol / maturation of 5.8S rRNA / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of ubiquitin protein ligase activity / negative regulation of NF-kappaB transcription factor activity / homeostatic process / macrophage chemotaxis / lung morphogenesis / male meiosis I / positive regulation of natural killer cell proliferation / ribosomal large subunit binding / Protein hydroxylation / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / cellular response to actinomycin D / blastocyst development / Response of EIF2AK4 (GCN2) to amino acid deficiency / positive regulation of glial cell proliferation / SRP-dependent cotranslational protein targeting to membrane / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of signal transduction by p53 class mediator / Viral mRNA Translation / protein transmembrane transporter activity / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / protein localization to nucleus / GTP hydrolysis and joining of the 60S ribosomal subunit / hematopoietic stem cell differentiation / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of protein binding / Major pathway of rRNA processing in the nucleolus and cytosol / ribosomal subunit export from nucleus / protein targeting / protein-RNA complex assembly / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / maturation of LSU-rRNA / rough endoplasmic reticulum / ERAD pathway / Maturation of protein E / Maturation of protein E / MDM2/MDM4 family protein binding 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
| ||||||||||||||||||
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. | ||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 8oj8.cif.gz | 3.6 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb8oj8.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8oj8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8oj8_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 8oj8_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 8oj8_validation.xml.gz | 220.3 KB | Display | |
| Data in CIF | 8oj8_validation.cif.gz | 392.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/8oj8 ftp://data.pdbj.org/pub/pdb/validation_reports/oj/8oj8 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 16908MC ![]() 8ohdC ![]() 8oj0C ![]() 8oj5C C: citing same article ( M: map data used to model this data |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
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 |
|---|---|
| #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) |
|---|---|
| #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 |
|---|---|
| #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 / |
|---|
-Details
| Has ligand of interest | N |
|---|
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component |
| ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Source (natural) |
| ||||||||||||||||||||||||
| 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 |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| 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) |
-
Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
|---|---|
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 20750 / Symmetry type: POINT |
Movie
Controller
About Yorodumi



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







PDBj




















































FIELD EMISSION GUN