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Yorodumi- PDB-8ops: Human terminal uridylyltransferase 7 (TUT7/ZCCHC6) bound with pre... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8ops | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Human terminal uridylyltransferase 7 (TUT7/ZCCHC6) bound with pre-let7g miRNA and Lin28A - complex 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | RNA / Polymerase / uridylation / RNA maturation and turnover control | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of glial cell differentiation / positive regulation of cell proliferation involved in kidney development / negative regulation of pre-miRNA processing / polyuridylation-dependent mRNA catabolic process / uridylyltransferase activity / transposable element silencing by mRNA destabilization / miRNA catabolic process / protein-RNA adaptor activity / RNA uridylyltransferase / RNA 3'-end processing ...negative regulation of glial cell differentiation / positive regulation of cell proliferation involved in kidney development / negative regulation of pre-miRNA processing / polyuridylation-dependent mRNA catabolic process / uridylyltransferase activity / transposable element silencing by mRNA destabilization / miRNA catabolic process / protein-RNA adaptor activity / RNA uridylyltransferase / RNA 3'-end processing / pre-miRNA binding / RNA uridylyltransferase activity / Transcriptional regulation of pluripotent stem cells / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / miRNA metabolic process / Deadenylation of mRNA / pre-miRNA processing / positive regulation of cytoplasmic translation / sequence-specific mRNA binding / oocyte maturation / miRNA binding / stem cell population maintenance / Zygotic genome activation (ZGA) / germ cell development / positive regulation of TOR signaling / rough endoplasmic reticulum / translation initiation factor binding / positive regulation of neuron differentiation / stem cell differentiation / cellular response to glucose stimulus / P-body / cytoplasmic stress granule / G-quadruplex RNA binding / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / negative regulation of translation / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.82 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Yi, G. / Ye, M. / Gilbert, R.J. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024Title: Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs. Authors: Gangshun Yi / Mingda Ye / Loic Carrique / Afaf El-Sagheer / Tom Brown / Chris J Norbury / Peijun Zhang / Robert J C Gilbert / ![]() Abstract: Tumor-suppressor let-7 pre-microRNAs (miRNAs) are regulated by terminal uridylyltransferases TUT7 and TUT4 that either promote let-7 maturation by adding a single uridine nucleotide to the pre-miRNA ...Tumor-suppressor let-7 pre-microRNAs (miRNAs) are regulated by terminal uridylyltransferases TUT7 and TUT4 that either promote let-7 maturation by adding a single uridine nucleotide to the pre-miRNA 3' end or mark them for degradation by the addition of multiple uridines. Oligo-uridylation is increased in cells by enhanced TUT7/4 expression and especially by the RNA-binding pluripotency factor LIN28A. Using cryogenic electron microscopy, we captured high-resolution structures of active forms of TUT7 alone, of TUT7 plus pre-miRNA and of both TUT7 and TUT4 bound with pre-miRNA and LIN28A. Our structures reveal that pre-miRNAs engage the enzymes in fundamentally different ways depending on the presence of LIN28A, which clamps them onto the TUTs to enable processive 3' oligo-uridylation. This study reveals the molecular basis for mono- versus oligo-uridylation by TUT7/4, as determined by the presence of LIN28A, and thus their mechanism of action in the regulation of cell fate and in cancer. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 | 8ops.cif.gz | 232.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ops.ent.gz | 167.5 KB | Display | PDB format |
| PDBx/mmJSON format | 8ops.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8ops_validation.pdf.gz | 988.1 KB | Display | wwPDB validaton report |
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| Full document | 8ops_full_validation.pdf.gz | 994.8 KB | Display | |
| Data in XML | 8ops_validation.xml.gz | 33.6 KB | Display | |
| Data in CIF | 8ops_validation.cif.gz | 48.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/op/8ops ftp://data.pdbj.org/pub/pdb/validation_reports/op/8ops | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 17086MC ![]() 8oefC ![]() 8oppC ![]() 8optC ![]() 8ostC 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
| #1: Protein | Mass: 171493.766 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TUT7, HS2, KIAA1711, ZCCHC6 / Production host: ![]() |
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| #2: Protein | Mass: 22778.975 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LIN28A, CSDD1, LIN28, ZCCHC1 / Production host: ![]() |
| #3: RNA chain | Mass: 22858.557 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
| #4: Chemical | ChemComp-ZN / |
| Has ligand of interest | N |
| Has protein modification | N |
-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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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
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| Buffer solution | pH: 7.8 | ||||||||||||||||||||||||
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.82 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 183972 / Symmetry type: POINT | ||||||||||||||||||||||||
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About Yorodumi



Homo sapiens (human)
United Kingdom, 1items
Citation








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FIELD EMISSION GUN