+Open data
-Basic information
Entry | Database: PDB / ID: 4ui9 | ||||||
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Title | Atomic structure of the human Anaphase-Promoting Complex | ||||||
Components |
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Keywords | CELL CYCLE / UBIQUITINATION / APC/C / APC SUBUNITS / ANAPHASE PROMOTING COMPLEX | ||||||
Function / homology | Function and homology information negative regulation of DNA endoreduplication / positive regulation of biomineral tissue development / negative regulation of meiotic nuclear division / positive regulation of anaphase-promoting complex-dependent catabolic process / negative regulation of mitotic metaphase/anaphase transition / positive regulation of mesenchymal stem cell migration / regulation of meiotic nuclear division / Mitotic Metaphase/Anaphase Transition / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase ...negative regulation of DNA endoreduplication / positive regulation of biomineral tissue development / negative regulation of meiotic nuclear division / positive regulation of anaphase-promoting complex-dependent catabolic process / negative regulation of mitotic metaphase/anaphase transition / positive regulation of mesenchymal stem cell migration / regulation of meiotic nuclear division / Mitotic Metaphase/Anaphase Transition / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / regulation of mitotic cell cycle spindle assembly checkpoint / protein branched polyubiquitination / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / vesicle organization / Phosphorylation of Emi1 / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of meiotic cell cycle / anaphase-promoting complex-dependent catabolic process / metaphase/anaphase transition of mitotic cell cycle / lens fiber cell differentiation / positive regulation of synaptic plasticity / regulation of exit from mitosis / anaphase-promoting complex binding / Phosphorylation of the APC/C / negative regulation of ubiquitin-protein transferase activity / positive regulation of mitotic metaphase/anaphase transition / positive regulation of ubiquitin protein ligase activity / ubiquitin ligase activator activity / spindle assembly involved in female meiosis I / protein K11-linked ubiquitination / meiotic spindle / enzyme-substrate adaptor activity / positive regulation of dendrite morphogenesis / regulation of mitotic metaphase/anaphase transition / oocyte maturation / ubiquitin-ubiquitin ligase activity / negative regulation of ubiquitin protein ligase activity / regulation of mitotic nuclear division / mitotic metaphase chromosome alignment / molecular function inhibitor activity / G1/S-Specific Transcription / regulation of DNA replication / mitotic G2 DNA damage checkpoint signaling / negative regulation of cellular senescence / microtubule polymerization / Regulation of APC/C activators between G1/S and early anaphase / cullin family protein binding / ubiquitin ligase inhibitor activity / Transcriptional Regulation by VENTX / ubiquitin-like ligase-substrate adaptor activity / positive regulation of axon extension / positive regulation of osteoblast differentiation / protein K48-linked ubiquitination / heterochromatin / Cyclin A:Cdk2-associated events at S phase entry / regulation of mitotic cell cycle / positive regulation of G2/M transition of mitotic cell cycle / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / nuclear periphery / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / Assembly of the pre-replicative complex / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / brain development / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / CDK-mediated phosphorylation and removal of Cdc6 / mitotic spindle / kinetochore / spindle / ubiquitin-protein transferase activity / Separation of Sister Chromatids / microtubule cytoskeleton / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / mitotic cell cycle / nervous system development / Senescence-Associated Secretory Phenotype (SASP) / ubiquitin-dependent protein catabolic process / protein phosphatase binding / nuclear membrane / molecular adaptor activity / cell differentiation / protein ubiquitination / cell division / negative regulation of gene expression / DNA repair / centrosome / DNA damage response / ubiquitin protein ligase binding / positive regulation of cell population proliferation / nucleolus / protein kinase binding / zinc ion binding / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||
Authors | Chang, L. / Zhang, Z. / Yang, J. / McLaughlin, S.H. / Barford, D. | ||||||
Citation | Journal: Nature / Year: 2015 Title: Atomic structure of the APC/C and its mechanism of protein ubiquitination. Authors: Leifu Chang / Ziguo Zhang / Jing Yang / Stephen H McLaughlin / David Barford / Abstract: The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the ...The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex and interphase early mitotic inhibitor 1 (Emi1) ensures the correct order and timing of distinct cell-cycle transitions. Here we use cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of future experiments to investigate APC/C functions in vivo. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 4ui9.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4ui9.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 4ui9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4ui9_validation.pdf.gz | 605.5 KB | Display | wwPDB validaton report |
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Full document | 4ui9_full_validation.pdf.gz | 887.5 KB | Display | |
Data in XML | 4ui9_validation.xml.gz | 184.3 KB | Display | |
Data in CIF | 4ui9_validation.cif.gz | 278.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ui/4ui9 ftp://data.pdbj.org/pub/pdb/validation_reports/ui/4ui9 | HTTPS FTP |
-Related structure data
Related structure data | 2924MC 2925C 2926C 5a31C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-ANAPHASE-PROMOTING COMPLEX SUBUNIT ... , 12 types, 13 molecules ABDEGILMNOWXY
#1: Protein | Mass: 216777.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9H1A4 |
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#2: Protein | Mass: 9866.702 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9NYG5 |
#4: Protein | Mass: 14302.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P60006 |
#5: Protein | Mass: 11677.995 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q96DE5 |
#7: Protein | Mass: 9808.025 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q8NHZ8 |
#8: Protein | Mass: 92205.195 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UJX5 |
#11: Protein | Mass: 21021.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UM13 |
#12: Protein | Mass: 8528.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9BS18 |
#13: Protein | Mass: 93938.977 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UJX6 |
#14: Protein | Mass: 85216.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UJX4 |
#19: Protein | Mass: 9793.999 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q8NHZ8 |
#20: Protein | Mass: 63106.809 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UJX3 |
-CELL DIVISION CYCLE PROTEIN ... , 4 types, 6 molecules CPFHJK
#3: Protein | Mass: 68356.406 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UJX2 #6: Protein | Mass: 92005.062 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P30260 #9: Protein | | Mass: 71747.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q13042 #10: Protein | | Mass: 71806.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q13042 |
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-Protein , 2 types, 2 molecules RS
#15: Protein | Mass: 54838.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UM11 |
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#16: Protein | Mass: 50297.645 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UKT4 |
-Protein/peptide , 2 types, 2 molecules TU
#17: Protein/peptide | Mass: 1609.780 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) |
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#18: Protein/peptide | Mass: 2258.669 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: Q9UKT4*PLUS |
-Non-polymers , 1 types, 5 molecules
#21: Chemical | ChemComp-ZN / |
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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 |
-Sample preparation
Component | Name: HUMAN ANAPHASE-PROMOTING COMPLEX / Type: COMPLEX |
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Buffer solution | pH: 8 |
Specimen | Conc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: HOLEY CARBON |
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Tecnai F30 / Image courtesy: FEI Company |
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Microscopy | Model: FEI TECNAI F30 / Date: Feb 9, 2014 |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 78000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm |
Image recording | Electron dose: 27 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
Radiation wavelength | Relative weight: 1 |
-Processing
EM software |
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Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||
3D reconstruction | Resolution: 3.6 Å / Num. of particles: 202084 / Nominal pixel size: 1.36 Å / Actual pixel size: 1.36 Å / Symmetry type: POINT | ||||||||||||
Refinement | Highest resolution: 3.6 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3.6 Å
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