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Open data
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Basic information
Entry | Database: PDB / ID: 6pto | ||||||||||||
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Title | Structure of Ctf4 trimer in complex with three CMG helicases | ||||||||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | 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 | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.9 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 20473MC ![]() 6ptjC ![]() 6ptnC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein , 3 types, 9 molecules XYZeErk5I
#1: Protein | Mass: 104543.391 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: CTF4, CHL15, POB1, YPR135W, P9659.7 / Production host: ![]() ![]() ![]() #6: Protein | Mass: 74324.836 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: CDC45, SLD4, YLR103C, L8004.11 / Production host: ![]() ![]() ![]() #10: Protein | ![]() Mass: 86505.734 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM5, CDC46, YLR274W, L9328.1 / Production host: ![]() ![]() ![]() ![]() |
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-DNA replication complex GINS protein ... , 4 types, 12 molecules nAaoBbpCcqDd
#2: Protein | Mass: 24230.576 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF1, YDR013W, PZA208, YD8119.18 / Production host: ![]() ![]() ![]() #3: Protein | Mass: 25096.807 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF2, YJL072C, HRF213, J1086 / Production host: ![]() ![]() ![]() #4: Protein | Mass: 21977.135 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF3, YOL146W / Production host: ![]() ![]() ![]() #5: Protein | Mass: 33983.617 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: SLD5, YDR489W / Production host: ![]() ![]() ![]() |
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-DNA replication licensing factor ... , 5 types, 15 molecules h2Fi3Gj4Hl6Jm7K
#7: Protein | Mass: 98911.539 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM2, YBL023C, YBL0438 / Production host: ![]() ![]() ![]() ![]() #8: Protein | Mass: 107653.508 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM3, YEL032W, SYGP-ORF23 / Production host: ![]() ![]() ![]() ![]() #9: Protein | Mass: 105138.375 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM4, CDC54, HCD21, YPR019W, YP9531.13 / Production host: ![]() ![]() ![]() ![]() #11: Protein | Mass: 113110.211 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM6, YGL201C / Production host: ![]() ![]() ![]() ![]() #12: Protein | Mass: 95049.875 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM7, CDC47, YBR202W, YBR1441 / Production host: ![]() ![]() ![]() ![]() |
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-Non-polymers , 1 types, 6 molecules ![](data/chem/img/ATP.gif)
#13: Chemical | ChemComp-ATP / ![]() |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: ![]() |
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Sample preparation
Component | Name: CMG-CMG-CMG-Ctf4 / Type: COMPLEX / Entity ID: #1-#12 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Specimen support | Details: unspecified |
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: FEI TITAN KRIOS |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction![]() | Resolution: 7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 53117 / Symmetry type: POINT |
Atomic model building | Protocol: RIGID BODY FIT |