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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-20472 | ||||||||||||
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Title | Structure of Ctf4 trimer in complex with two CMG helicases | ||||||||||||
![]() | primary map | ||||||||||||
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Function / homology | ![]() establishment of sister chromatid cohesion / Unwinding of DNA / Cul8-RING ubiquitin ligase complex / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / MCM complex binding / GINS complex / DNA strand elongation involved in mitotic DNA replication / nuclear DNA replication ...establishment of sister chromatid cohesion / Unwinding of DNA / Cul8-RING ubiquitin ligase complex / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / MCM complex binding / GINS complex / DNA strand elongation involved in mitotic DNA replication / nuclear DNA replication / mitotic DNA replication preinitiation complex assembly / premeiotic DNA replication / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / mitotic DNA replication / Activation of the pre-replicative complex / CMG complex / nuclear pre-replicative complex / MCM complex / Activation of ATR in response to replication stress / DNA replication preinitiation complex / replication fork protection complex / double-strand break repair via break-induced replication / mitotic DNA replication initiation / single-stranded DNA helicase activity / silent mating-type cassette heterochromatin formation / regulation of DNA-templated DNA replication initiation / mitotic sister chromatid cohesion / DNA strand elongation involved in DNA replication / nuclear chromosome / DNA unwinding involved in DNA replication / nuclear replication fork / DNA replication origin binding / DNA replication initiation / subtelomeric heterochromatin formation / DNA helicase activity / helicase activity / transcription elongation by RNA polymerase II / heterochromatin formation / DNA-templated DNA replication / nucleosome assembly / mitotic cell cycle / single-stranded DNA binding / DNA helicase / chromosome, telomeric region / DNA repair / DNA damage response / chromatin binding / ATP hydrolysis activity / nucleoplasm / ATP binding / identical protein binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 5.8 Å | ||||||||||||
![]() | Yuan Z / Georgescu R / Bai L / Santos R / Donnell M / Li H | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Ctf4 organizes sister replisomes and Pol α into a replication factory. Authors: Zuanning Yuan / Roxana Georgescu / Ruda de Luna Almeida Santos / Daniel Zhang / Lin Bai / Nina Y Yao / Gongpu Zhao / Michael E O'Donnell / Huilin Li / ![]() Abstract: The current view is that eukaryotic replisomes are independent. Here we show that Ctf4 tightly dimerizes CMG helicase, with an extensive interface involving Psf2, Cdc45, and Sld5. Interestingly, Ctf4 ...The current view is that eukaryotic replisomes are independent. Here we show that Ctf4 tightly dimerizes CMG helicase, with an extensive interface involving Psf2, Cdc45, and Sld5. Interestingly, Ctf4 binds only one Pol α-primase. Thus, Ctf4 may have evolved as a trimer to organize two helicases and one Pol α-primase into a replication factory. In the 2CMG-Ctf4-1Pol α-primase factory model, the two CMGs nearly face each other, placing the two lagging strands toward the center and two leading strands out the sides. The single Pol α-primase is centrally located and may prime both sister replisomes. The Ctf4-coupled-sister replisome model is consistent with cellular microscopy studies revealing two sister forks of an origin remain attached and are pushed forward from a protein platform. The replication factory model may facilitate parental nucleosome transfer during replication. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 20.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 29.2 KB 29.2 KB | Display Display | ![]() |
Images | ![]() | 123.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ptnMC ![]() 6ptjC ![]() 6ptoC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | primary map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.074 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : CMG-Ctf4
+Supramolecule #1: CMG-Ctf4
+Macromolecule #1: DNA polymerase alpha-binding protein
+Macromolecule #2: DNA replication complex GINS protein PSF1
+Macromolecule #3: DNA replication complex GINS protein PSF2
+Macromolecule #4: DNA replication complex GINS protein PSF3
+Macromolecule #5: DNA replication complex GINS protein SLD5
+Macromolecule #6: Cell division control protein 45
+Macromolecule #7: DNA replication licensing factor MCM2
+Macromolecule #8: DNA replication licensing factor MCM3
+Macromolecule #9: DNA replication licensing factor MCM4
+Macromolecule #10: Minichromosome maintenance protein 5
+Macromolecule #11: DNA replication licensing factor MCM6
+Macromolecule #12: DNA replication licensing factor MCM7
+Macromolecule #13: ADENOSINE-5'-TRIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 5.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 53853 |
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Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-6ptn: |