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Yorodumi- EMDB-16902: 60S ribosomal subunit bound to the E3-UFM1 complex - state 2 (native) -
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Open data
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Basic information
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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 / negative regulation of protein serine/threonine kinase activity / UFM1 transferase 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 / negative regulation of protein serine/threonine kinase activity / UFM1 transferase activity / positive regulation of protein localization to endoplasmic reticulum / positive regulation of proteolysis involved in protein catabolic process / protein K69-linked ufmylation / protein ufmylation / negative regulation of protein kinase activity by regulation of protein phosphorylation / 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 / 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 / positive regulation of cell cycle G1/S phase transition / negative regulation of T cell mediated immune response to tumor cell / protein localization to endoplasmic reticulum / 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 / positive regulation of proteasomal protein catabolic process / axial mesoderm development / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / post-translational protein targeting to membrane, translocation / regulation of cyclin-dependent protein serine/threonine kinase activity / ribosomal protein import into nucleus / mitotic G2/M transition checkpoint / 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 / cartilage development / Transferases; Acyltransferases; Aminoacyltransferases / ribosome disassembly / response to L-glutamate / regulation of canonical NF-kappaB signal transduction / GAIT complex / mitogen-activated protein kinase binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / TORC2 complex binding / alpha-beta T cell differentiation / G1 to G0 transition / regulation of neuron differentiation / 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 / negative regulation of protein import into nucleus / homeostatic process / macrophage chemotaxis / negative regulation of PERK-mediated unfolded protein response / lung morphogenesis / mitotic G2 DNA damage checkpoint signaling / negative regulation of protein phosphorylation / male meiosis I / negative regulation of MAP kinase activity / positive regulation of natural killer cell proliferation / ribosomal large subunit binding / Protein hydroxylation / ubiquitin-like protein ligase binding / 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 Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) / Homo sapiens environmental sample (environmental samples) | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||
Authors | Penchev I / DaRosa PA / Becker T / Beckmann R / Kopito R | ||||||||||||||||||
| Funding support | European Union, Germany, United Kingdom, United States, 5 items
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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. | ||||||||||||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_16902.map.gz | 484.9 MB | EMDB map data format | |
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| Header (meta data) | emd-16902-v30.xml emd-16902.xml | 80.9 KB 80.9 KB | Display Display | EMDB header |
| Images | emd_16902.png | 65.3 KB | ||
| Filedesc metadata | emd-16902.cif.gz | 16.5 KB | ||
| Others | emd_16902_half_map_1.map.gz emd_16902_half_map_2.map.gz | 486.9 MB 486.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16902 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16902 | HTTPS FTP |
-Validation report
| Summary document | emd_16902_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_16902_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_16902_validation.xml.gz | 19.5 KB | Display | |
| Data in CIF | emd_16902_validation.cif.gz | 23.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16902 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16902 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8oj0MC ![]() 8ohdC ![]() 8oj5C ![]() 8oj8C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_16902.map.gz / Format: CCP4 / Size: 600.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.727 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_16902_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_16902_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : 60S ribosomal subunit bound to the E3-UFM1 complex and Sec61
+Supramolecule #1: 60S ribosomal subunit bound to the E3-UFM1 complex and Sec61
+Supramolecule #2: 60S ribosomal subunit
+Supramolecule #3: E3 UFM1-protein ligase 1
+Macromolecule #1: Protein transport protein Sec61 subunit alpha isoform 1
+Macromolecule #2: Protein transport protein Sec61 subunit gamma
+Macromolecule #3: Protein transport protein Sec61 subunit beta
+Macromolecule #7: E3 UFM1-protein ligase 1
+Macromolecule #8: CDK5 regulatory subunit-associated protein 3
+Macromolecule #9: DDRGK domain-containing protein 1
+Macromolecule #10: Ubiquitin-fold modifier 1
+Macromolecule #11: Eukaryotic translation initiation factor 6
+Macromolecule #12: 60S ribosomal protein L8
+Macromolecule #13: 60S ribosomal protein L3
+Macromolecule #14: 60S ribosomal protein L4
+Macromolecule #15: 60S ribosomal protein L5
+Macromolecule #16: 60S ribosomal protein L6
+Macromolecule #17: 60S ribosomal protein L7
+Macromolecule #18: 60S ribosomal protein L7a
+Macromolecule #19: 60S ribosomal protein L9
+Macromolecule #20: Ribosomal protein uL16-like
+Macromolecule #21: 60S ribosomal protein L11
+Macromolecule #22: 60S ribosomal protein L13
+Macromolecule #23: 60S ribosomal protein L14
+Macromolecule #24: 60S ribosomal protein L15
+Macromolecule #25: 60S ribosomal protein L13a
+Macromolecule #26: 60S ribosomal protein L17
+Macromolecule #27: 60S ribosomal protein L18
+Macromolecule #28: 60S ribosomal protein L19
+Macromolecule #29: 60S ribosomal protein L18a
+Macromolecule #30: 60S ribosomal protein L21
+Macromolecule #31: 60S ribosomal protein L22
+Macromolecule #32: 60S ribosomal protein L23
+Macromolecule #33: 60S ribosomal protein L24
+Macromolecule #34: 60S ribosomal protein L23a
+Macromolecule #35: 60S ribosomal protein L26
+Macromolecule #36: 60S ribosomal protein L27
+Macromolecule #37: 60S ribosomal protein L27a
+Macromolecule #38: 60S ribosomal protein L29
+Macromolecule #39: 60S ribosomal protein L30
+Macromolecule #40: 60S ribosomal protein L31
+Macromolecule #41: 60S ribosomal protein L32
+Macromolecule #42: 60S ribosomal protein L35a
+Macromolecule #43: 60S ribosomal protein L34
+Macromolecule #44: 60S ribosomal protein L35
+Macromolecule #45: 60S ribosomal protein L36
+Macromolecule #46: 60S ribosomal protein L37
+Macromolecule #47: 60S ribosomal protein L38
+Macromolecule #48: 60S ribosomal protein L39
+Macromolecule #49: Ubiquitin-60S ribosomal protein L40
+Macromolecule #50: 60S ribosomal protein L36a
+Macromolecule #51: 60S ribosomal protein L37a
+Macromolecule #52: 60S ribosomal protein L28
+Macromolecule #53: 60S ribosomal protein L10a
+Macromolecule #4: 28S rRNA
+Macromolecule #5: 5S rRNA
+Macromolecule #6: 5.8S rRNA
+Macromolecule #54: MAGNESIUM ION
+Macromolecule #55: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: OTHER |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 20377 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Germany,
United Kingdom,
United States, 5 items
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FIELD EMISSION GUN
