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Open data
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Basic information
| Entry | Database: PDB / ID: 5a31 | ||||||
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| Title | Structure of the human APC-Cdh1-Hsl1-UbcH10 complex. | ||||||
Components |
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Keywords | CELL CYCLE / UBIQUITINATION / APC/C | ||||||
| Function / homology | Function and homology informationnegative regulation of mitotic spindle pole body separation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / positive regulation of mitotic actomyosin contractile ring contraction / deactivation of mitotic spindle assembly checkpoint / positive regulation of anaphase-promoting complex-dependent catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of exit from mitosis / free ubiquitin chain polymerization / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase ...negative regulation of mitotic spindle pole body separation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / positive regulation of mitotic actomyosin contractile ring contraction / deactivation of mitotic spindle assembly checkpoint / positive regulation of anaphase-promoting complex-dependent catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of exit from mitosis / free ubiquitin chain polymerization / 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 / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / positive regulation of synaptic plasticity / 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 / protein branched polyubiquitination / Phosphorylation of the APC/C / anaphase-promoting complex binding / regulation of exit from mitosis / positive regulation of dendrite morphogenesis / positive regulation of mitotic metaphase/anaphase transition / positive regulation of ubiquitin protein ligase activity / (E3-independent) E2 ubiquitin-conjugating enzyme / exit from mitosis / ubiquitin ligase activator activity / positive regulation of ubiquitin-dependent protein catabolic process / protein K11-linked ubiquitination / regulation of mitotic metaphase/anaphase transition / ubiquitin-ubiquitin ligase activity / E2 ubiquitin-conjugating enzyme / mitotic metaphase chromosome alignment / ubiquitin conjugating enzyme activity / Regulation of APC/C activators between G1/S and early anaphase / ubiquitin-like protein ligase binding / cullin family protein binding / Transcriptional Regulation by VENTX / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin ligase complex / enzyme-substrate adaptor activity / positive regulation of axon extension / protein K48-linked ubiquitination / heterochromatin / intercellular bridge / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / nuclear periphery / cyclin binding / regulation of mitotic cell cycle / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Assembly of the pre-replicative complex / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / G protein-coupled receptor binding / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / brain development / kinetochore / CDK-mediated phosphorylation and removal of Cdc6 / spindle / protein polyubiquitination / neuron projection development / ubiquitin-protein transferase activity / positive regulation of protein catabolic process / mitotic spindle / Separation of Sister Chromatids / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / nervous system development / mitotic cell cycle / microtubule cytoskeleton / Senescence-Associated Secretory Phenotype (SASP) / ubiquitin-dependent protein catabolic process / protein phosphatase binding / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / cell differentiation / protein ubiquitination / negative regulation of gene expression / cell division / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / centrosome / nucleolus / zinc ion binding / nucleoplasm / ATP binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | HOMO SAPIENS (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||
Authors | Chang, L. / Zhang, Z. / Yang, J. / Mclaughlin, S.H. / Barford, D. | ||||||
Citation | Journal: Nature / Year: 2015Title: 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. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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| PDBx/mmCIF format | 5a31.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb5a31.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 5a31.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5a31_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 5a31_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 5a31_validation.xml.gz | 227.9 KB | Display | |
| Data in CIF | 5a31_validation.cif.gz | 351.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a3/5a31 ftp://data.pdbj.org/pub/pdb/validation_reports/a3/5a31 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2925MC ![]() 2924C ![]() 2926C ![]() 4ui9C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
-ANAPHASE-PROMOTING COMPLEX SUBUNIT ... , 14 types, 17 molecules ABDEFHGWIJKLMNOXY
| #1: Protein | Mass: 159616.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9H1A4*PLUS | ||||||||||||||||||
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| #2: Protein | Mass: 9866.702 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9NYG5 | ||||||||||||||||||
| #4: Protein | Mass: 14302.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P60006 | ||||||||||||||||||
| #5: Protein | Mass: 11677.995 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q96DE5 | ||||||||||||||||||
| #6: Protein | Mass: 92005.125 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P30260#7: Protein | Mass: 9793.999 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q8NHZ8#8: Protein | | Mass: 92205.195 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UJX5#9: Protein | | Mass: 71631.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q13042#10: Protein | | Mass: 71806.672 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q13042#11: Protein | | Mass: 21282.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UM13#12: Protein | | Mass: 8528.309 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q2NKV2, UniProt: Q9BS18*PLUS#13: Protein | | Mass: 79116.469 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UJX6*PLUS#14: Protein | | Mass: 85087.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UJX4#20: Protein | Mass: 66832.164 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UJX3 |
-Protein , 2 types, 3 molecules CPQ
| #3: Protein | Mass: 68905.008 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9UJX2#15: Protein | | Mass: 17793.396 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper)References: UniProt: O00762*PLUS, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme, E2 ubiquitin-conjugating enzyme |
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-THE ANAPHASE-PROMOTING COMPLEX CHAIN ... , 4 types, 4 molecules RTUV
| #16: Protein | Mass: 42944.512 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P53197*PLUS |
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| #17: Protein/peptide | Mass: 1876.293 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) |
| #18: Protein/peptide | Mass: 2060.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) |
| #19: Protein/peptide | Mass: 1421.707 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: TRICHOPLUSIA NI (cabbage looper) |
-Non-polymers , 1 types, 3 molecules 
| #21: Chemical |
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-Details
| Sequence details | THE CHAINS A AND N CORRESPOND TO UNIPROT Q9H1A4 AND Q9UJX6 RESPECTIVELY. CHAIN Q RESIDUES 1-179 AND ...THE CHAINS A AND N CORRESPOND |
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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: 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 |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI F30 / Date: Jul 12, 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: 16 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
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Processing
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| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||
| 3D reconstruction | Resolution: 4.3 Å / Num. of particles: 19939 / Nominal pixel size: 1.36 Å / Actual pixel size: 1.36 Å / Symmetry type: POINT | ||||||||||||
| Refinement | Highest resolution: 4.3 Å | ||||||||||||
| Refinement step | Cycle: LAST / Highest resolution: 4.3 Å
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TRICHOPLUSIA NI (cabbage looper)
