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Open data
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Basic information
| Entry | Database: PDB / ID: 9th8 | ||||||||||||
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| Title | Cryo-EM structure of MCM2-7 DH bound to Sld3-Sld7, Cdc45 and DNA | ||||||||||||
Components |
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Keywords | REPLICATION / Helicase / Activation / Phosphorylation | ||||||||||||
| Function / homology | Function and homology informationregulation of mitotic DNA replication initiation / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / mitotic DNA replication preinitiation complex assembly / MCM complex binding / nuclear DNA replication / premeiotic DNA replication / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / Activation of the pre-replicative complex ...regulation of mitotic DNA replication initiation / MCM core complex / Assembly of the pre-replicative complex / Switching of origins to a post-replicative state / mitotic DNA replication preinitiation complex assembly / MCM complex binding / nuclear DNA replication / premeiotic DNA replication / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / Activation of the pre-replicative complex / nuclear pre-replicative complex / CMG complex / Activation of ATR in response to replication stress / DNA replication preinitiation complex / mitotic DNA replication checkpoint signaling / double-strand break repair via break-induced replication / MCM complex / mitotic DNA replication initiation / mitotic DNA replication / silent mating-type cassette heterochromatin formation / single-stranded DNA helicase activity / DNA strand elongation involved in DNA replication / nuclear replication fork / DNA replication origin binding / subtelomeric heterochromatin formation / chromosome, centromeric region / DNA replication initiation / regulation of DNA-templated DNA replication initiation / DNA helicase activity / helicase activity / transcription elongation by RNA polymerase II / spindle pole / nuclear envelope / peroxisome / single-stranded DNA binding / heterochromatin formation / DNA helicase / DNA replication / chromosome, telomeric region / chromatin binding / DNA damage response / chromatin / endoplasmic reticulum / ATP hydrolysis activity / nucleoplasm / zinc ion binding / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||||||||
Authors | Saleh, A. / Noguchi, Y. / Schneider, S. / Aramayo, R. / Speck, C. | ||||||||||||
| Funding support | United Kingdom, 3items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural insights into Sld3-Sld7-dependent Cdc45 loading during replication initiation Authors: Noguchi, Y. / Saleh, A. / Schneider, S. / Ivanova, M.E. / Chen, Z.A. / Ranjha, L. / Aramayo, R. / Tognetti, S. / Faull, S.V. / Rappsilber, J. / Speck, C. | ||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9th8.cif.gz | 1.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9th8.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9th8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/th/9th8 ftp://data.pdbj.org/pub/pdb/validation_reports/th/9th8 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 55918MC ![]() 9tgdC ![]() 9tgmC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-DNA chain , 2 types, 2 molecules OS
| #1: DNA chain | Mass: 18491.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
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| #2: DNA chain | Mass: 18491.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
-DNA replication licensing factor ... , 5 types, 10 molecules B2C3D4F6G7
| #3: Protein | Mass: 98911.539 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM2, YBL023C, YBL0438 / Production host: ![]() #4: Protein | Mass: 107653.508 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM3, YEL032W, SYGP-ORF23 / Production host: ![]() #5: Protein | Mass: 105138.375 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM4, CDC54, HCD21, YPR019W, YP9531.13 / Production host: ![]() #7: Protein | Mass: 113110.211 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM6, YGL201C / Production host: ![]() #8: Protein | Mass: 95049.875 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM7, CDC47, YBR202W, YBR1441 / Production host: ![]() |
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-Protein , 4 types, 5 molecules E5XZY
| #6: Protein | Mass: 86505.734 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: MCM5, CDC46, YLR274W, L9328.1 / Production host: ![]() #9: Protein | | Mass: 77428.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SLD3, YGL113W, G2980 / Production host: ![]() #10: Protein | | Mass: 74324.836 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: CDC45, SLD4, YLR103C, L8004.11 / Production host: ![]() #11: Protein | | Mass: 29598.828 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SLD7, YOR060C, YOR29-11 / Production host: ![]() |
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-Non-polymers , 2 types, 18 molecules 


| #12: Chemical | ChemComp-ADP / #13: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: MCM2-7 DH bound to Sld3-Sld7, Cdc45 and DNA / Type: COMPLEX / Entity ID: #1-#11 / Source: RECOMBINANT |
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| Molecular weight | Value: 1.65 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K Details: Wait time: 30 s Blotting time: 1.5 s Blot force: +2 |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company | |||||||||||||||||||||
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| Microscopy | Model: TFS KRIOS | |||||||||||||||||||||
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM | |||||||||||||||||||||
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE | |||||||||||||||||||||
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER | |||||||||||||||||||||
| Image recording |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C2 (2 fold cyclic) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 292336 Details: For the composite MSC map, resolution was estimated with phenix.mtriage, using the unmasked model-map FSC, which gave an FSC(0.143) resolution of 2.9 Angstrom. Final focused refinement ...Details: For the composite MSC map, resolution was estimated with phenix.mtriage, using the unmasked model-map FSC, which gave an FSC(0.143) resolution of 2.9 Angstrom. Final focused refinement particle subsets used to generate composite map (292,336 particles): DH core (38,859 particles) Sld3 MRD1/2:Mcm4/6 (149,668 particles) Sld3-Cdc45:Mcm2/5 (52,475 particles) Sld7:Mcm6 (51,334 particles) Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building |
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| Refinement | Highest resolution: 2.9 Å / Cross valid method: NONE Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






United Kingdom, 3items
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FIELD EMISSION GUN





