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Yorodumi- PDB-8oj8: 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) -
+Open data
-Basic information
Entry | Database: PDB / ID: 8oj8 | ||||||||||||||||||
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Title | 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native) | ||||||||||||||||||
Components |
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Keywords | RIBOSOME / ER / UFMylation / recycling | ||||||||||||||||||
Function / homology | Function and homology information UFM1 ligase activity / positive regulation of reticulophagy / UFM1 transferase activity / protein ufmylation / protein K69-linked ufmylation / positive regulation of proteolysis involved in protein catabolic process / endoplasmic reticulum Sec complex / negative regulation of IRE1-mediated unfolded protein response / pronephric nephron development / endoplasmic reticulum quality control compartment ...UFM1 ligase activity / positive regulation of reticulophagy / UFM1 transferase activity / protein ufmylation / protein K69-linked ufmylation / positive regulation of proteolysis involved in protein catabolic process / endoplasmic reticulum Sec complex / negative regulation of IRE1-mediated unfolded protein response / pronephric nephron development / endoplasmic reticulum quality control compartment / regulation of proteasomal ubiquitin-dependent protein catabolic process / cotranslational protein targeting to membrane / lamin filament / Ssh1 translocon complex / negative regulation of T cell mediated immune response to tumor cell / Sec61 translocon complex / regulation of fatty acid biosynthetic process / protein targeting to ER / regulation of megakaryocyte differentiation / protein insertion into ER membrane / negative regulation of T cell activation / miRNA-mediated post-transcriptional gene silencing / regulation of intracellular estrogen receptor signaling pathway / ribosome disassembly / miRNA-mediated gene silencing by inhibition of translation / SRP-dependent cotranslational protein targeting to membrane, translocation / eukaryotic 80S initiation complex / negative regulation of protein neddylation / translation at presynapse / axial mesoderm development / ribosomal protein import into nucleus / negative regulation of formation of translation preinitiation complex / 90S preribosome assembly / signal sequence binding / post-translational protein targeting to membrane, translocation / TORC2 complex binding / Transferases; Acyltransferases; Aminoacyltransferases / GAIT complex / regulation of canonical NF-kappaB signal transduction / middle ear morphogenesis / reticulophagy / regulation of glycolytic process / maturation of 5.8S rRNA / A band / regulation of reactive oxygen species metabolic process / alpha-beta T cell differentiation / cytoplasmic side of rough endoplasmic reticulum membrane / regulation of G1 to G0 transition / epidermal growth factor binding / exit from mitosis / 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 / response to L-glutamate / protein-DNA complex disassembly / retrograde protein transport, ER to cytosol / positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / negative regulation of ubiquitin protein ligase activity / optic nerve development / negative regulation of NF-kappaB transcription factor activity / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / response to aldosterone / retinal ganglion cell axon guidance / homeostatic process / G1 to G0 transition / macrophage chemotaxis / lung morphogenesis / male meiosis I / Protein hydroxylation / ribosomal large subunit binding / Peptide chain elongation / preribosome, large subunit precursor / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / Formation of a pool of free 40S subunits / blastocyst development / ubiquitin ligase inhibitor activity / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / protein transmembrane transporter activity / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / protein localization to nucleus / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / hematopoietic stem cell differentiation / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / protein targeting / protein-RNA complex assembly / cellular response to interleukin-4 / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / cellular response to actinomycin D / negative regulation of ubiquitin-dependent protein catabolic process / ribosomal subunit export from nucleus / positive regulation of autophagy / rough endoplasmic reticulum / positive regulation of glial cell proliferation / ERAD pathway / MDM2/MDM4 family protein binding / Maturation of protein E 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: 2024 Title: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-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
Summary document | 8oj8_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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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 (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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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 |
-Sample preparation
Component |
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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 |
-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) |
-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 |