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Open data
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Basic information
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Title | Cryo-EM structure of CDK2-cyclin A in complex with CDC25A | |||||||||
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![]() | cell-cycle / CDK / phosphatase / cancer / CELL CYCLE | |||||||||
Function / homology | ![]() positive regulation of G2/MI transition of meiotic cell cycle / cell cycle G1/S phase transition / mitotic cell cycle phase transition / Transcription of E2F targets under negative control by DREAM complex / Polo-like kinase mediated events / cyclin-dependent protein serine/threonine kinase regulator activity / regulation of cyclin-dependent protein serine/threonine kinase activity / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex ...positive regulation of G2/MI transition of meiotic cell cycle / cell cycle G1/S phase transition / mitotic cell cycle phase transition / Transcription of E2F targets under negative control by DREAM complex / Polo-like kinase mediated events / cyclin-dependent protein serine/threonine kinase regulator activity / regulation of cyclin-dependent protein serine/threonine kinase activity / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / G2 Phase / cyclin-dependent protein kinase activity / Y chromosome / Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes / positive regulation of heterochromatin formation / p53-Dependent G1 DNA Damage Response / X chromosome / PTK6 Regulates Cell Cycle / regulation of DNA replication / regulation of anaphase-promoting complex-dependent catabolic process / Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / phosphoprotein phosphatase activity / centrosome duplication / Telomere Extension By Telomerase / G0 and Early G1 / Activation of the pre-replicative complex / cellular response to nitric oxide / cyclin-dependent protein kinase holoenzyme complex / cyclin-dependent kinase / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Activation of ATR in response to replication stress / Cyclin E associated events during G1/S transition / Cyclin A/B1/B2 associated events during G2/M transition / Cajal body / Cyclin A:Cdk2-associated events at S phase entry / condensed chromosome / mitotic G1 DNA damage checkpoint signaling / regulation of mitotic cell cycle / regulation of G2/M transition of mitotic cell cycle / positive regulation of G2/M transition of mitotic cell cycle / cyclin binding / protein-tyrosine-phosphatase / post-translational protein modification / : / meiotic cell cycle / positive regulation of DNA replication / protein tyrosine phosphatase activity / male germ cell nucleus / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / potassium ion transport / response to radiation / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / Meiotic recombination / SCF(Skp2)-mediated degradation of p27/p21 / Orc1 removal from chromatin / G1/S transition of mitotic cell cycle / Transcriptional regulation of granulopoiesis / G2/M transition of mitotic cell cycle / Cyclin D associated events in G1 / cellular response to UV / cellular senescence / Regulation of TP53 Degradation / nuclear envelope / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / protein-folding chaperone binding / Senescence-Associated Secretory Phenotype (SASP) / regulation of gene expression / peptidyl-serine phosphorylation / DNA replication / Regulation of TP53 Activity through Phosphorylation / cell population proliferation / transcription regulator complex / Ras protein signal transduction / chromosome, telomeric region / Ub-specific processing proteases / endosome / chromatin remodeling / protein domain specific binding / cell division / protein phosphorylation / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / DNA-templated transcription / centrosome / positive regulation of cell population proliferation / protein kinase binding / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / magnesium ion binding / signal transduction / nucleoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||
![]() | Rowland RJ / Noble MEM / Endicott JA | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the CDK2-cyclin A-CDC25A Complex Authors: Rowland RJ / Korolchuk S / Salamina M / Ault JR / Hart S / Turkenburg JP / Blaza JN / Noble MEM / Endicott JA | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 85.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21 KB 21 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.5 KB | Display | ![]() |
Images | ![]() | 122.1 KB | ||
Masks | ![]() | 91.1 MB | ![]() | |
Filedesc metadata | ![]() | 6.9 KB | ||
Others | ![]() ![]() | 84.6 MB 84.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 805.5 KB | Display | ![]() |
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Full document | ![]() | 805.1 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 22.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8rozMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Voxel size | X=Y=Z: 0.825 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
File | emd_19408_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_19408_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Trimeric complex of CDK2-cyclin A-CDC25A
Entire | Name: Trimeric complex of CDK2-cyclin A-CDC25A |
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Components |
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-Supramolecule #1: Trimeric complex of CDK2-cyclin A-CDC25A
Supramolecule | Name: Trimeric complex of CDK2-cyclin A-CDC25A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 86 KDa |
-Macromolecule #1: Cyclin-dependent kinase 2
Macromolecule | Name: Cyclin-dependent kinase 2 / type: protein_or_peptide / ID: 1 Details: Human cyclin dependant protein kinase 2 (CDK2) phosphorylated at Tyr15 and Thr160 Number of copies: 1 / Enantiomer: LEVO / EC number: cyclin-dependent kinase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 34.136449 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MENFQKVEKI GEGT(PTR)GVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLLDVI HTENKL YLV FEFLHQDLKK FMDASALTGI PLPLIKSYLF QLLQGLAFCH SHRVLHRDLK PQNLLINTEG AIKLADFGLA RAFGVPV RT Y(TPO) ...String: MENFQKVEKI GEGT(PTR)GVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLLDVI HTENKL YLV FEFLHQDLKK FMDASALTGI PLPLIKSYLF QLLQGLAFCH SHRVLHRDLK PQNLLINTEG AIKLADFGLA RAFGVPV RT Y(TPO)HEVVTLWY RAPEILLGCK YYSTAVDIWS LGCIFAEMVT RRALFPGDSE IDQLFRIFRT LGTPDEVVWP GVTS MPDYK PSFPKWARQD FSKVVPPLDE DGRSLLSQML HYDPNKRISA KAALAHPFFQ DVTKPVPHLR L UniProtKB: Cyclin-dependent kinase 2 |
-Macromolecule #2: Cyclin-A2
Macromolecule | Name: Cyclin-A2 / type: protein_or_peptide / ID: 2 / Details: Bovine cyclin A2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 30.119799 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGVNEVPDYH EDIHTYLREM EVKCKPKVGY MKKQPDITNS MRAILVDWLV EVGEEYKLQN ETLHLAVNYI DRFLSSMSVL RGKLQLVGT AAMLLASKFE EIYPPEVAEF VYITDDTYTK KQVLRMEHLV LKVLAFDLAA PTINQFLTQY FLHQQPANCK V ESLAMFLG ...String: MGVNEVPDYH EDIHTYLREM EVKCKPKVGY MKKQPDITNS MRAILVDWLV EVGEEYKLQN ETLHLAVNYI DRFLSSMSVL RGKLQLVGT AAMLLASKFE EIYPPEVAEF VYITDDTYTK KQVLRMEHLV LKVLAFDLAA PTINQFLTQY FLHQQPANCK V ESLAMFLG ELSLIDADPY LKYLPSVIAA AAFHLALYTV TGQSWPESLV QKTGYTLETL KPCLLDLHQT YLRAPQHAQQ SI REKYKNS KYHGVSLLNP PETLNV UniProtKB: Cyclin-A2 |
-Macromolecule #3: M-phase inducer phosphatase 1
Macromolecule | Name: M-phase inducer phosphatase 1 / type: protein_or_peptide / ID: 3 Details: M-phase inducer phosphatase 1 (CDC25A) catalytic domain Number of copies: 1 / Enantiomer: LEVO / EC number: protein-tyrosine-phosphatase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 22.533123 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SMVIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGK RVIVVFHSEF SSERGPRMCR YVRERDRLGN EYPKLHYPEL YVLKGGYKEF FMKCQSYCEP PSYRPMHHED F KEDLKKFR TKSRTWAGEK SKREMYSRLK KL UniProtKB: M-phase inducer phosphatase 1 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.8 mg/mL | ||||||||||||
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Buffer | pH: 7.4 Component:
Details: 50 mM HEPES, 200 mM NaCl, 1 mM DTT, pH 7.4 | ||||||||||||
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.026000000000000002 kPa Details: Grids were glow discharged for 1min at 20 mAmp/0.26 mBar | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average exposure time: 1.92 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 150000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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Details | A model was generated using ModelAngelo. Initial local fitting was performed in ChimerX followed by real space refinement in Phenix and manual fitting in coot. |
Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 144 |
Output model | ![]() PDB-8roz: |