|Entry||Database: EMDB / ID: 6535|
|Title||Structure of the eukaryotic replicative CMG helicase and pumpjack motion|
|Map data||Structure of CMG with "Flat" Mcm2-7 ring|
|Sample||Saccharomyces cerevisiae CMG complex:|
|Keywords||CMG helicase / Cryo-EM|
|Function / homology||AAA+ ATPase domain / DNA replication licensing factor Mcm7 / MCM domain / CDC45 family / GINS complex, subunit Psf1 / DNA replication complex GINS protein Psf2 / DNA replication licensing factor Mcm2 / DNA replication licensing factor Mcm3 / Mini-chromosome maintenance complex protein 4 / DNA replication licensing factor Mcm5 ...AAA+ ATPase domain / DNA replication licensing factor Mcm7 / MCM domain / CDC45 family / GINS complex, subunit Psf1 / DNA replication complex GINS protein Psf2 / DNA replication licensing factor Mcm2 / DNA replication licensing factor Mcm3 / Mini-chromosome maintenance complex protein 4 / DNA replication licensing factor Mcm5 / DNA replication licensing factor Mcm6 / GINS complex subunit Sld5 / GINS complex protein Sld5, alpha-helical domain / GINS complex, subunit Psf3 / Nucleic acid-binding, OB-fold / Mini-chromosome maintenance, conserved site / GINS subunit, domain A / P-loop containing nucleoside triphosphate hydrolase / MCM N-terminal domain / Mini-chromosome maintenance protein / DNA replication complex GINS protein SLD5, C-terminal / MCM OB domain / GINS, helical bundle-like domain superfamily / MCM P-loop domain / GINS complex, subunit Psf3 superfamily / Mini-chromosome maintenance protein 2 / GINS complex protein / MCM N-terminal domain / Switching of origins to a post-replicative state / DNA replication complex GINS protein SLD5 C-terminus / MCM OB domain / MCM family signature. / Activation of the pre-replicative complex / MCM family domain profile. / CDC45-like protein / Orc1 removal from chromatin / DNA strand elongation involved in mitotic DNA replication / GINS complex / mitotic DNA replication preinitiation complex assembly / MCM complex binding / negative regulation of ATP-dependent DNA helicase activity / MCM core complex / CMG complex / nuclear DNA replication / regulation of chromatin silencing at telomere / negative regulation of chromatin silencing at telomere / MCM complex / establishment of chromatin silencing / mitotic DNA replication initiation / pre-replicative complex assembly involved in nuclear cell cycle DNA replication / regulation of DNA-dependent DNA replication initiation / nuclear pre-replicative complex / DNA replication preinitiation complex / 3'-5' DNA helicase activity / single-stranded DNA-dependent ATPase activity / double-strand break repair via break-induced replication / nuclear replication fork / DNA strand elongation involved in DNA replication / replication fork protection complex / chromatin silencing at silent mating-type cassette / DNA duplex unwinding / DNA helicase activity / DNA unwinding involved in DNA replication / positive regulation of G1/S transition of mitotic cell cycle / chromatin silencing at telomere / DNA replication origin binding / DNA replication initiation / DNA helicase / helicase activity / chromosome, telomeric region / single-stranded DNA binding / DNA-dependent DNA replication / nuclear chromosome, telomeric region / cellular response to DNA damage stimulus / chromatin binding / nucleoplasm / ATP binding / nucleus / metal ion binding / cytoplasm / DNA replication licensing factor MCM3 / DNA replication licensing factor MCM2 / Minichromosome maintenance protein 5 / DNA replication licensing factor MCM4 / DNA replication licensing factor MCM7 / DNA replication complex GINS protein PSF2 / DNA replication licensing factor MCM6 / DNA replication complex GINS protein SLD5 / Cell division control protein 45 / DNA replication complex GINS protein PSF3 / DNA replication complex GINS protein PSF1|
Function and homology information
|Source||Saccharomyces cerevisiae (baker's yeast)|
|Method||single particle reconstruction / cryo EM / 4.7 Å resolution|
|Authors||Yuan Z / Bai L / Sun J / Georgescu RE / Liu J / O'Donnell ME / Li H|
|Citation||Journal: Nat. Struct. Mol. Biol. / Year: 2016|
Title: Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation.
Authors: Zuanning Yuan / Lin Bai / Jingchuan Sun / Roxana Georgescu / Jun Liu / Michael E O'Donnell / Huilin Li
|Validation Report||PDB-ID: 3jc5|
SummaryFull reportAbout validation report
|Date||Deposition: Nov 23, 2015 / Header (metadata) release: Feb 10, 2016 / Map release: Feb 10, 2016 / Last update: Apr 27, 2016|
|Structure viewer||EM map: |
Downloads & links
|File||emd_6535.map.gz (map file in CCP4 format, 65537 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.01 Å|
CCP4 map header:
-Entire Saccharomyces cerevisiae CMG complex
|Entire||Name: Saccharomyces cerevisiae CMG complex / Number of components: 1|
|Mass||Theoretical: 700 kDa|
-Component #1: protein, CMG complex
|Protein||Name: CMG complex / a.k.a: CMG / Recombinant expression: Yes / Number of Copies: 1|
|Mass||Theoretical: 700 kDa|
|Source||Species: Saccharomyces cerevisiae (baker's yeast)|
|Source (engineered)||Expression System: Saccharomyces cerevisiae (baker's yeast)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.6 mg/ml|
Buffer solution: 20 mM Tris acetate, 40 mM potassium glutamate, 2 mM DTT, 0.1 mM EDTA
|Support film||400 mesh holey carbon C-flat grid, glow-discharged in air|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % / Method: Blot for 3 seconds before plunging|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: Aug 1, 2015|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 50 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 29000 X (nominal), 49505 X (calibrated) / Imaging mode: BRIGHT FIELD / Defocus: 1500 - 3500 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of digital images: 8000|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 178530|
Details: All steps, including automatic particle picking, 2D classification, 3D classification, and 3D refinement were performed in Relion 1.4.
|3D reconstruction||Software: Relion_1.4 / CTF correction: CTFFIND4 / Resolution: 4.7 Å / Resolution method: FSC 0.143, gold-standard|
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