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Yorodumi- PDB-6d6v: CryoEM structure of Tetrahymena telomerase with telomeric DNA at ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6d6v | ||||||||||||||||||||||||||||||
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Title | CryoEM structure of Tetrahymena telomerase with telomeric DNA at 4.8 Angstrom resolution | ||||||||||||||||||||||||||||||
Components |
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Keywords | REPLICATION / Telomerase / telomere | ||||||||||||||||||||||||||||||
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 RNA binding / telomerase holoenzyme complex / 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 RNA binding / telomerase holoenzyme complex / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / DNA recombination / DNA replication / chromosome, telomeric region / DNA repair / DNA binding / zinc ion binding / metal ion binding Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | Tetrahymena thermophila (eukaryote) | ||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.8 Å | ||||||||||||||||||||||||||||||
Authors | Jiang, J. / Wang, Y. / Susac, L. / Chan, H. / Basu, R. / Zhou, Z.H. / Feigon, J. | ||||||||||||||||||||||||||||||
Funding support | United States, 9items
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Citation | Journal: Cell / Year: 2018 Title: Structure of Telomerase with Telomeric DNA. Authors: Jiansen Jiang / Yaqiang Wang / Lukas Sušac / Henry Chan / Ritwika Basu / Z Hong Zhou / Juli Feigon / Abstract: Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA ...Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA (TER). Its activity is a critical determinant of human health, affecting aging, cancer, and stem cell renewal. Lack of atomic models of telomerase, particularly one with DNA bound, has limited our mechanistic understanding of telomeric DNA repeat synthesis. We report the 4.8 Å resolution cryoelectron microscopy structure of active Tetrahymena telomerase bound to telomeric DNA. The catalytic core is an intricately interlocked structure of TERT and TER, including a previously structurally uncharacterized TERT domain that interacts with the TEN domain to physically enclose TER and regulate activity. This complete structure of a telomerase catalytic core and its interactions with telomeric DNA from the template to telomere-interacting p50-TEB complex provides unanticipated insights into telomerase assembly and catalytic cycle and a new paradigm for a reverse transcriptase RNP. | ||||||||||||||||||||||||||||||
History |
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-Structure visualization
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Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 6d6v.cif.gz | 428.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6d6v.ent.gz | 319.9 KB | Display | PDB format |
PDBx/mmJSON format | 6d6v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6d6v_validation.pdf.gz | 994.7 KB | Display | wwPDB validaton report |
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Full document | 6d6v_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6d6v_validation.xml.gz | 62.8 KB | Display | |
Data in CIF | 6d6v_validation.cif.gz | 95.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d6/6d6v ftp://data.pdbj.org/pub/pdb/validation_reports/d6/6d6v | HTTPS FTP |
-Related structure data
Related structure data | 7821MC 7820C C: citing same article (ref.) M: map data used to model this data |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 2 types, 2 molecules AH
#1: Protein | Mass: 133486.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: UniProt: O77448, RNA-directed DNA polymerase |
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#8: Protein | Mass: 64207.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: UniProt: Q6JXI6, UniProt: W7X6T2*PLUS |
-Telomerase-associated protein ... , 2 types, 2 molecules DG
#2: Protein | Mass: 82040.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: UniProt: D2CVN6 |
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#7: Protein | Mass: 13379.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) |
-Telomerase holoenzyme ... , 2 types, 2 molecules FE
#3: Protein | Mass: 14007.626 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: UniProt: A0A0U8UFF4 |
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#4: Protein | Mass: 30993.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: UniProt: A0A0U8TRG9 |
-RNA chain / DNA chain / Non-polymers , 3 types, 3 molecules BC
#5: RNA chain | Mass: 50746.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / References: GenBank: 15148878 |
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#6: DNA chain | Mass: 6059.875 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Tetrahymena thermophila (eukaryote) |
#9: Chemical | ChemComp-ZN / |
-Details
Sequence details | THE AUTHORS STATE THAT FOR P50 THEY WERE ONLY ABLE TO TRACE THE PROTEIN BACKBONE IN THE DENSITY ...THE AUTHORS STATE THAT FOR P50 THEY WERE ONLY ABLE TO TRACE THE PROTEIN BACKBONE IN THE DENSITY CORRESPOND |
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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 | Name: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA Type: COMPLEX / Entity ID: #1-#8 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Tetrahymena thermophila (eukaryote) |
Buffer solution | pH: 8 |
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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Average exposure time: 12 sec. / Electron dose: 52 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.12_2829: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 52506 / Symmetry type: POINT | ||||||||||||||||||||||||
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