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- PDB-3jc6: Structure of the eukaryotic replicative CMG helicase and pumpjack... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3jc6 | ||||||||||||||||||||||||||||||||||||||||||||||||
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Title | Structure of the eukaryotic replicative CMG helicase and pumpjack motion | ||||||||||||||||||||||||||||||||||||||||||||||||
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Function / homology | MCM6 C-terminal winged-helix domain / GINS complex subunit Sld5 / MCM N-terminal domain / P-loop containing nucleoside triphosphate hydrolase / GINS subunit, domain A / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
Specimen source | ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Li, H. / Bai, L. / Yuan, Z. / Sun, J. / Georgescu, R.E. / Liu, J. / O'Donnell, M.E. | ||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Journal: Nat. Struct. Mol. Biol. / Year: 2016 Title: Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation. ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
Validation Report | ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
Date | Deposition: Nov 24, 2015 / Release: Feb 10, 2016
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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 | ![]() ![]() |
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PDB format | ![]() ![]() |
PDBML Plus | ![]() |
Others | ![]() |
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Links
-Related structure data
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Assembly
Deposited unit | ![]()
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Components
-DNA replication licensing factor ... , 5 types, 5 molecules 23467
#1: Protein/peptide | Mass: 98911.539 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM2, YBL023C, YBL0438 ![]() ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 107653.508 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM3, YEL032W, SYGP-ORF23 / Production host: ![]() ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 105138.375 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM4, CDC54, HCD21, YPR019W, YP9531.13 / Production host: ![]() ![]() ![]() ![]() |
#5: Protein/peptide | Mass: 113110.211 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM6, YGL201C ![]() ![]() ![]() ![]() ![]() |
#6: Protein/peptide | Mass: 95049.875 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM7, CDC47, YBR202W, YBR1441 / Production host: ![]() ![]() ![]() ![]() |
-Protein/peptide , 2 types, 2 molecules 5E
#4: Protein/peptide | ![]() Mass: 86505.734 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: MCM5, CDC46, YLR274W, L9328.1 / Production host: ![]() ![]() ![]() ![]() |
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#7: Protein/peptide | Mass: 77043.539 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: CDC45, SLD4, YLR103C, L8004.11 / Production host: ![]() ![]() ![]() |
-DNA replication complex GINS protein ... , 4 types, 4 molecules DBAC
#8: Protein/peptide | Mass: 33983.617 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: SLD5, YDR489W / Production host: ![]() ![]() ![]() |
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#9: Protein/peptide | Mass: 25096.807 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF2, YJL072C, HRF213, J1086 / Production host: ![]() ![]() ![]() |
#10: Protein/peptide | Mass: 24230.576 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF1, YDR013W, PZA208, YD8119.18 / Production host: ![]() ![]() ![]() |
#11: Protein/peptide | Mass: 21977.135 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: PSF3, YOL146W / Production host: ![]() ![]() ![]() |
-Non-polymers , 1 types, 1 molecules 
#12: Chemical | ChemComp-ZN / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / Reconstruction method: ![]() |
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Sample preparation
Component | Name: Saccharomyces cerevisiae CMG complex / Type: COMPLEX |
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Molecular weight | Value: 0.7 MDa / Experimental value: NO |
Buffer solution | Name: 20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA Details: 20 mM Tris acetate, pH 7.5, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA pH: 7.5 |
Specimen | Conc.: 0.6 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Specimen support | Details: 400 mesh holey carbon C-flat grid, glow-discharged in air |
Vitrification![]() | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % Details: Blot for 3 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). Method: Blot for 3 seconds before plunging |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Microscope model: FEI TITAN KRIOS / Date: Aug 1, 2015 |
Electron gun | Electron source: FIELD EMISSION GUN![]() |
Electron lens | Mode: BRIGHT FIELD![]() ![]() |
Specimen holder | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
Image scans | Number digital images: 8000 |
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Processing
EM software |
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CTF correction![]() | Details: CTFFIND4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Method: Single particle reconstruction![]() Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 469818 / Nominal pixel size: 1.01 / Actual pixel size: 1.01 Details: (Single particle details: All steps, including automatic particle picking, 2D classification, 3D classification, and 3D refinement were performed in Relion 1.4.) (Single particle--Applied symmetry: C1) Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Details: REFINEMENT PROTOCOL--rigid body / Ref protocol: RIGID BODY FIT / Ref space: REAL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 2Q9Q | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine | Overall SU ML: 1.1 / Sigma F: 0 / Overall phase error: 42.73 / Stereochemistry target values: MLHL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent shrinkage radii: 0.9 Å / Solvent vdw probe radii: 1.11 Å / Solvent model details: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | B iso max: 381.32 Å2 / B iso mean: 144.6555 Å2 / B iso min: 3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Least-squares process | R factor R free![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine hist #LAST | Highest resolution: 3.7 Å / Lowest resolution: 258.56 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Number of atoms included #LAST | Protein: 23731 / Nucleic acid: 0 / Ligand: 1 / Solvent: 0 / Total: 23732 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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Refine LS shell | Refine ID: ELECTRON MICROSCOPY / Total number of bins used: 14
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