+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-21565 | |||||||||||||||||||||
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Title | Arm conformation from CST-3xTEL oligomer-mixture | |||||||||||||||||||||
Map data | Arm conformation from CST-3xTEL oligomer-mixture | |||||||||||||||||||||
Sample |
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Biological species | Homo sapiens (human) | |||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 9.2 Å | |||||||||||||||||||||
Authors | Lim C / Barbour AT / Zaug AJ / Goodrich KJ / McKay AE / Wuttke DS / Cech TR | |||||||||||||||||||||
Funding support | United States, 6 items
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Citation | Journal: Science / Year: 2020 Title: The structure of human CST reveals a decameric assembly bound to telomeric DNA. Authors: Ci Ji Lim / Alexandra T Barbour / Arthur J Zaug / Karen J Goodrich / Allison E McKay / Deborah S Wuttke / Thomas R Cech / Abstract: The CTC1-STN1-TEN1 (CST) complex is essential for telomere maintenance and resolution of stalled replication forks genome-wide. Here, we report the 3.0-angstrom cryo-electron microscopy structure of ...The CTC1-STN1-TEN1 (CST) complex is essential for telomere maintenance and resolution of stalled replication forks genome-wide. Here, we report the 3.0-angstrom cryo-electron microscopy structure of human CST bound to telomeric single-stranded DNA (ssDNA), which assembles as a decameric supercomplex. The atomic model of the 134-kilodalton CTC1 subunit, built almost entirely de novo, reveals the overall architecture of CST and the DNA-binding anchor site. The carboxyl-terminal domain of STN1 interacts with CTC1 at two separate docking sites, allowing allosteric mediation of CST decamer assembly. Furthermore, ssDNA appears to staple two monomers to nucleate decamer assembly. CTC1 has stronger structural similarity to Replication Protein A than the expected similarity to yeast Cdc13. The decameric structure suggests that CST can organize ssDNA analogously to the nucleosome's organization of double-stranded DNA. | |||||||||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_21565.map.gz | 5.2 MB | EMDB map data format | |
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Header (meta data) | emd-21565-v30.xml emd-21565.xml | 10.4 KB 10.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_21565_fsc.xml | 9.2 KB | Display | FSC data file |
Images | emd_21565.png | 80 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-21565 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21565 | HTTPS FTP |
-Validation report
Summary document | emd_21565_validation.pdf.gz | 78.8 KB | Display | EMDB validaton report |
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Full document | emd_21565_full_validation.pdf.gz | 77.9 KB | Display | |
Data in XML | emd_21565_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21565 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21565 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_21565.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Arm conformation from CST-3xTEL oligomer-mixture | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.219 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Arm conformation of CST monomer from CST-3xTEL oligomer-mixture
Entire | Name: Arm conformation of CST monomer from CST-3xTEL oligomer-mixture |
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Components |
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-Supramolecule #1: Arm conformation of CST monomer from CST-3xTEL oligomer-mixture
Supramolecule | Name: Arm conformation of CST monomer from CST-3xTEL oligomer-mixture type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
Molecular weight | Experimental: 200 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TECNAI F20 |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |