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Open data
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Basic information
Entry | Database: PDB / ID: 8a61 | |||||||||
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Title | S. cerevisiae apo phosphorylated APC/C | |||||||||
![]() | (Anaphase-promoting complex subunit ...) x 13 | |||||||||
![]() | CELL CYCLE / APC/C / ubiqutiniation / D-box / Cdh1 | |||||||||
Function / homology | ![]() anaphase-promoting complex assembly / negative regulation of anaphase-promoting complex-dependent catabolic process / positive regulation of mitotic actomyosin contractile ring contraction / deactivation of mitotic spindle assembly checkpoint / ascospore wall assembly / Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) / anaphase-promoting complex / regulation of meiotic cell cycle / metaphase/anaphase transition of mitotic cell cycle / anaphase-promoting complex-dependent catabolic process ...anaphase-promoting complex assembly / negative regulation of anaphase-promoting complex-dependent catabolic process / positive regulation of mitotic actomyosin contractile ring contraction / deactivation of mitotic spindle assembly checkpoint / ascospore wall assembly / Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) / anaphase-promoting complex / regulation of meiotic cell cycle / metaphase/anaphase transition of mitotic cell cycle / anaphase-promoting complex-dependent catabolic process / positive regulation of mitotic metaphase/anaphase transition / protein K11-linked ubiquitination / positive regulation of protein autoubiquitination / reciprocal meiotic recombination / regulation of mitotic metaphase/anaphase transition / exit from mitosis / ligase activity / mitotic sister chromatid segregation / cullin family protein binding / ubiquitin ligase inhibitor activity / Antigen processing: Ubiquitination & Proteasome degradation / enzyme regulator activity / negative regulation of DNA-templated DNA replication initiation / regulation of mitotic cell cycle / cyclin binding / nuclear periphery / kinetochore / spindle pole / ubiquitin protein ligase activity / chromatin organization / ubiquitin-dependent protein catabolic process / molecular adaptor activity / protein ubiquitination / cell cycle / cell division / ubiquitin protein ligase binding / mitochondrion / zinc ion binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.4 Å | |||||||||
![]() | Barford, D. / Fernandez-Vazquez, E. / Zhang, Z. / Yang, J. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the S. cerevisiae apo phosphorylated APC/C Authors: Barford, D. / Fernandez-Vazquez, E. / Zhang, Z. / Yang, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.5 MB | Display | ![]() |
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PDB format | ![]() | 1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 997.6 KB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 169.9 KB | Display | |
Data in CIF | ![]() | 242.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 15201MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Anaphase-promoting complex subunit ... , 13 types, 17 molecules FHJKGWETUCODPINQA
#1: Protein | Mass: 85487.391 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: CDC27, APC3, SNB1, YBL084C, YBL0718 / Production host: ![]() #2: Protein | Mass: 96282.266 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: CDC16, YKL022C / Production host: ![]() #3: Protein | Mass: 14096.860 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: CDC26, HIT3, SCD26, YFR036W / Production host: ![]() #4: Protein | | Mass: 30901.439 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC9, YLR102C / Production host: ![]() #5: Protein | | Mass: 100099.570 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC2, RSI1, YLR127C, L3105, L3108 / Production host: ![]() #6: Protein | | Mass: 18887.105 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC11, YDL008W, D2900 / Production host: ![]() References: UniProt: Q12157, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) #7: Protein | | Mass: 196372.766 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC1, YNL172W, N1677 / Production host: ![]() #8: Protein | | Mass: 79355.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC5, RMC1, YOR249C / Production host: ![]() #9: Protein | Mass: 73197.984 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: CDC23, YHR166C / Production host: ![]() #10: Protein | | Mass: 19377.910 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: SWM1, APC13, YDR260C, YD9320A.11, YD9320A.11c / Production host: ![]() #11: Protein | | Mass: 42881.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: MND2, YIR025W / Production host: ![]() #12: Protein | | Mass: 75345.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: APC4, YDR118W / Production host: ![]() #13: Protein | | Mass: 28810.664 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: DOC1, APC10, YGL240W, HRC283 / Production host: ![]() |
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-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: Phosphorylated apo anaphase promoting complex/cyclosome (APC/C) Type: COMPLEX Details: Phosphorylated apo anaphase promoting complex/cyclosome (APC/C) Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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Molecular weight | Value: 1.127 MDa / Experimental value: NO | |||||||||||||||
Source (natural) | Organism: ![]() ![]() | |||||||||||||||
Source (recombinant) | Organism: ![]() | |||||||||||||||
Buffer solution | pH: 8.3 | |||||||||||||||
Buffer component |
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Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | |||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 K / Details: Blotting 2 secs |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 59000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 1600 nm / Calibrated defocus min: 2600 nm / Calibrated defocus max: 3900 nm / C2 aperture diameter: 51 µm / Alignment procedure: BASIC |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 70 K / Temperature (min): 70 K |
Image recording | Average exposure time: 2 sec. / Electron dose: 59 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 5904 |
Image scans | Sampling size: 1.7 µm / Width: 1034 / Height: 1034 |
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Processing
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 806068 | |||||||||||||||||||||||||||
3D reconstruction | Resolution: 5.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 287434 / Num. of class averages: 1 / Symmetry type: POINT | |||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | |||||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | |||||||||||||||||||||||||||
Displacement parameters | Biso mean: 251.66 Å2 | |||||||||||||||||||||||||||
Refine LS restraints |
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