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Yorodumi- EMDB-29903: Structure of LARP7 protein p65-telomerase RNA complex in telomerase -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-29903 | |||||||||
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Title | Structure of LARP7 protein p65-telomerase RNA complex in telomerase | |||||||||
Map data | ||||||||||
Sample |
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Keywords | La protein / La-related protein / telomerase / ribonucleoprotein / RNA BINDING PROTEIN | |||||||||
Function / homology | Function and homology information telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / : / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase ...telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / : / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / chromosome, telomeric region / DNA replication / DNA recombination / DNA repair / DNA binding / zinc ion binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Tetrahymena thermophila (eukaryote) / synthetic construct (others) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
Authors | Wang Y / He Y / Yang Y / Singh M / Eichhorn CD / Zhou ZH / Feigon J | |||||||||
Funding support | United States, 2 items
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Citation | Journal: J Mol Biol / Year: 2023 Title: Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR. Authors: Yaqiang Wang / Yao He / Yanjiao Wang / Yuan Yang / Mahavir Singh / Catherine D Eichhorn / Xinyi Cheng / Yi Xiao Jiang / Z Hong Zhou / Juli Feigon / Abstract: La-related protein 7 (LARP7) are a family of RNA chaperones that protect the 3'-end of RNA and are components of specific ribonucleoprotein complexes (RNP). In Tetrahymena thermophila telomerase, ...La-related protein 7 (LARP7) are a family of RNA chaperones that protect the 3'-end of RNA and are components of specific ribonucleoprotein complexes (RNP). In Tetrahymena thermophila telomerase, LARP7 protein p65 together with telomerase reverse transcriptase (TERT) and telomerase RNA (TER) form the core RNP. p65 has four known domains-N-terminal domain (NTD), La motif (LaM), RNA recognition motif 1 (RRM1), and C-terminal xRRM2. To date, only the xRRM2 and LaM and their interactions with TER have been structurally characterized. Conformational dynamics leading to low resolution in cryo-EM density maps have limited our understanding of how full-length p65 specifically recognizes and remodels TER for telomerase assembly. Here, we combined focused classification of Tetrahymena telomerase cryo-EM maps with NMR spectroscopy to determine the structure of p65-TER. Three previously unknown helices are identified, one in the otherwise intrinsically disordered NTD that binds the La module, one that extends RRM1, and another preceding xRRM2, that stabilize p65-TER interactions. The extended La module (αN, LaM and RRM1) interacts with the four 3' terminal U nucleotides, while LaM and αN additionally interact with TER pseudoknot, and LaM with stem 1 and 5' end. Our results reveal the extensive p65-TER interactions that promote TER 3'-end protection, TER folding, and core RNP assembly and stabilization. The structure of full-length p65 with TER also sheds light on the biological roles of genuine La and LARP7 proteins as RNA chaperones and core RNP components. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_29903.map.gz | 49.4 MB | EMDB map data format | |
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Header (meta data) | emd-29903-v30.xml emd-29903.xml | 23 KB 23 KB | Display Display | EMDB header |
Images | emd_29903.png | 70.1 KB | ||
Filedesc metadata | emd-29903.cif.gz | 7.8 KB | ||
Others | emd_29903_half_map_1.map.gz emd_29903_half_map_2.map.gz | 49.6 MB 49.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-29903 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-29903 | HTTPS FTP |
-Related structure data
Related structure data | 8gapMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_29903.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.36 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_29903_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_29903_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : tetrahymena telomerase holoenzyme
+Supramolecule #1: tetrahymena telomerase holoenzyme
+Macromolecule #1: Telomerase reverse transcriptase
+Macromolecule #2: Telomerase holoenzyme Teb1 subunit
+Macromolecule #3: Telomerase holoenzyme Teb2 subunit
+Macromolecule #4: Telomerase holoenzyme Teb3 subunit
+Macromolecule #5: Telomerase associated protein p50
+Macromolecule #8: Telomerase La-related protein p65
+Macromolecule #6: telomere DNA
+Macromolecule #7: Telomerase RNA
+Macromolecule #9: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: EMDB MAP EMDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 162358 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |