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- PDB-5g04: Structure of the human APC-Cdc20-Hsl1 complex -

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Entry
Database: PDB / ID: 5g04
TitleStructure of the human APC-Cdc20-Hsl1 complex
Components
  • (ANAPHASE-PROMOTING COMPLEX SUBUNIT ...) x 11
  • (CELL DIVISION CYCLE PROTEIN ...) x 4
  • PROBABLE SERINE/THREONINE-PROTEIN KINASE HSL1
KeywordsCELL CYCLE / PHOSPHORYLATION / MITOSIS / UBIQUITINATION
Function / homology
Function and homology information


negative regulation of diacylglycerol biosynthetic process / protein localization to septin ring / mitotic morphogenesis checkpoint signaling / cellular bud neck septin ring / metaphase/anaphase transition of cell cycle / metaphase/anaphase transition of meiosis I / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of anaphase-promoting complex-dependent catabolic process / positive regulation of synapse maturation ...negative regulation of diacylglycerol biosynthetic process / protein localization to septin ring / mitotic morphogenesis checkpoint signaling / cellular bud neck septin ring / metaphase/anaphase transition of cell cycle / metaphase/anaphase transition of meiosis I / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of anaphase-promoting complex-dependent catabolic process / positive regulation of synapse maturation / regulation of meiotic nuclear division / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / regulation of mitotic cell cycle spindle assembly checkpoint / regulation of dendrite development / 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 / 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 / protein branched polyubiquitination / Phosphorylation of the APC/C / anaphase-promoting complex binding / regulation of exit from mitosis / cellular bud neck / positive regulation of dendrite morphogenesis / positive regulation of mitotic metaphase/anaphase transition / positive regulation of ubiquitin protein ligase activity / ubiquitin ligase activator activity / protein K11-linked ubiquitination / regulation of mitotic metaphase/anaphase transition / ubiquitin-ubiquitin ligase activity / mitotic sister chromatid cohesion / mitotic metaphase chromosome alignment / mitotic spindle assembly checkpoint signaling / Regulation of APC/C activators between G1/S and early anaphase / Transcriptional Regulation by VENTX / cullin family protein binding / mitotic spindle assembly / enzyme-substrate adaptor activity / positive regulation of axon extension / ubiquitin-like ligase-substrate adaptor activity / protein K48-linked ubiquitination / heterochromatin / intercellular bridge / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / nuclear periphery / regulation of mitotic cell cycle / Resolution of Sister Chromatid Cohesion / 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 / protein catabolic process / RHO GTPases Activate Formins / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / G protein-coupled receptor binding / brain development / kinetochore / CDK-mediated phosphorylation and removal of Cdc6 / G2/M transition of mitotic cell cycle / histone deacetylase binding / spindle / neuron projection development / spindle pole / ubiquitin-protein transferase activity / 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 / cell differentiation / non-specific serine/threonine protein kinase / protein kinase activity / regulation of cell cycle / Ub-specific processing proteases / protein ubiquitination / negative regulation of gene expression / cell division / protein serine kinase activity / intracellular membrane-bounded organelle / protein serine/threonine kinase activity / positive regulation of cell population proliferation / ubiquitin protein ligase binding / centrosome / nucleolus
Similarity search - Function
: / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 15 / : / CDC20/Fizzy WD40 domain / The WD repeat Cdc20/Fizzy family / : / APC4, WD40 domain C-terminal half / Anaphase-promoting complex subunit 4, metazoa / Anaphase-promoting complex subunit 1, C-terminal ...: / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 15 / : / CDC20/Fizzy WD40 domain / The WD repeat Cdc20/Fizzy family / : / APC4, WD40 domain C-terminal half / Anaphase-promoting complex subunit 4, metazoa / Anaphase-promoting complex subunit 1, C-terminal / Anaphase-promoting complex subunit 1, middle domain / : / : / : / Anaphase-promoting complex subunit 1 WD40 beta-propeller domain / Anaphase-promoting complex sub unit 1 C-terminal domain / Anaphase-promoting complex subunit 1 middle domain / APC1 beta sandwich domain / Anaphase-promoting complex subunit 5, N-terminal domain / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex, subunit 16 / Cdc23 / Apc13 / Anaphase promoting complex subunit 8 / Cdc23 / Apc13p protein / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 4 long domain / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 5 domain / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex, cyclosome, subunit 4 / Anaphase-promoting complex subunit APC10/Doc1 / Anaphase-promoting complex, subunit CDC26 / Anaphase-promoting complex APC subunit CDC26 / Anaphase-promoting complex subunit 11, RING-H2 finger / Anaphase-promoting complex subunit 11 RING-H2 finger / Anaphase-promoting complex subunit 2, C-terminal / Anaphase-promoting complex subunit 2 / Anaphase promoting complex (APC) subunit 2 / Anaphase promoting complex (APC) subunit 2 / APC10/DOC domain / Anaphase-promoting complex, subunit 10 (APC10) / DOC domain profile. / Anaphase-promoting complex, subunit 10 (APC10) / Anaphase-promoting complex, cyclosome, subunit 3 / TPR repeat / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Tetratricopeptide repeat / : / Cullin / Tetratricopeptide repeat / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin alpha solenoid domain / Cullin family profile. / Tetratricopeptide repeat / Tetratricopeptide repeat domain / Zinc/RING finger domain, C3HC4 (zinc finger) / Tetratricopeptide repeat / Herpes Virus-1 / Galactose-binding domain-like / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / YVTN repeat-like/Quinoprotein amine dehydrogenase / Tetratricopeptide repeat / 7 Propeller / Methylamine Dehydrogenase; Chain H / Galactose-binding-like domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Armadillo-like helical / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / WD domain, G-beta repeat / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / Trp-Asp (WD) repeats signature. / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Jelly Rolls / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / Protein kinase domain / Winged helix-like DNA-binding domain superfamily / WD40-repeat-containing domain superfamily / Serine/Threonine protein kinases, catalytic domain / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich
Similarity search - Domain/homology
Cell division cycle protein 27 homolog / Probable serine/threonine-protein kinase HSL1 / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 11 ...Cell division cycle protein 27 homolog / Probable serine/threonine-protein kinase HSL1 / Anaphase-promoting complex subunit 15 / Cell division cycle protein 20 homolog / Cell division cycle protein 16 homolog / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 11 / Cell division cycle protein 23 homolog / Anaphase-promoting complex subunit 7 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 2 / Anaphase-promoting complex subunit 10
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
SACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsZhang, S. / Chang, L. / Alfieri, C. / Zhang, Z. / Yang, J. / Maslen, S. / Skehel, M. / Barford, D.
CitationJournal: Nature / Year: 2016
Title: Molecular mechanism of APC/C activation by mitotic phosphorylation.
Authors: Suyang Zhang / Leifu Chang / Claudio Alfieri / Ziguo Zhang / Jing Yang / Sarah Maslen / Mark Skehel / David Barford /
Abstract: In eukaryotes, the anaphase-promoting complex (APC/C, also known as the cyclosome) regulates the ubiquitin-dependent proteolysis of specific cell-cycle proteins to coordinate chromosome segregation ...In eukaryotes, the anaphase-promoting complex (APC/C, also known as the cyclosome) regulates the ubiquitin-dependent proteolysis of specific cell-cycle proteins to coordinate chromosome segregation in mitosis and entry into the G1 phase. The catalytic activity of the APC/C and its ability to specify the destruction of particular proteins at different phases of the cell cycle are controlled by its interaction with two structurally related coactivator subunits, Cdc20 and Cdh1. Coactivators recognize substrate degrons, and enhance the affinity of the APC/C for its cognate E2 (refs 4-6). During mitosis, cyclin-dependent kinase (Cdk) and polo-like kinase (Plk) control Cdc20- and Cdh1-mediated activation of the APC/C. Hyperphosphorylation of APC/C subunits, notably Apc1 and Apc3, is required for Cdc20 to activate the APC/C, whereas phosphorylation of Cdh1 prevents its association with the APC/C. Since both coactivators associate with the APC/C through their common C-box and Ile-Arg tail motifs, the mechanism underlying this differential regulation is unclear, as is the role of specific APC/C phosphorylation sites. Here, using cryo-electron microscopy and biochemical analysis, we define the molecular basis of how phosphorylation of human APC/C allows for its control by Cdc20. An auto-inhibitory segment of Apc1 acts as a molecular switch that in apo unphosphorylated APC/C interacts with the C-box binding site and obstructs engagement of Cdc20. Phosphorylation of the auto-inhibitory segment displaces it from the C-box-binding site. Efficient phosphorylation of the auto-inhibitory segment, and thus relief of auto-inhibition, requires the recruitment of Cdk-cyclin in complex with a Cdk regulatory subunit (Cks) to a hyperphosphorylated loop of Apc3. We also find that the small-molecule inhibitor, tosyl-l-arginine methyl ester, preferentially suppresses APC/C(Cdc20) rather than APC/C(Cdh1), and interacts with the binding sites of both the C-box and Ile-Arg tail motifs. Our results reveal the mechanism for the regulation of mitotic APC/C by phosphorylation and provide a rationale for the development of selective inhibitors of this state.
History
DepositionMar 16, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 25, 2016Provider: repository / Type: Initial release
Revision 1.1May 8, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_image_scans / pdbx_validate_polymer_linkage / refine / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_validate_polymer_linkage.dist / _pdbx_validate_polymer_linkage.label_alt_id_1 / _refine.ls_d_res_high / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

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Assembly

Deposited unit
A: ANAPHASE-PROMOTING COMPLEX SUBUNIT 1
B: ANAPHASE-PROMOTING COMPLEX SUBUNIT 11
C: CELL DIVISION CYCLE PROTEIN 23 HOMOLOG
D: ANAPHASE-PROMOTING COMPLEX SUBUNIT 15
E: ANAPHASE-PROMOTING COMPLEX SUBUNIT 16
F: CELL DIVISION CYCLE PROTEIN 27 HOMOLOG
G: ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26
H: CELL DIVISION CYCLE PROTEIN 27 HOMOLOG
I: ANAPHASE-PROMOTING COMPLEX SUBUNIT 4
J: CELL DIVISION CYCLE PROTEIN 16 HOMOLOG
K: CELL DIVISION CYCLE PROTEIN 16 HOMOLOG
L: ANAPHASE-PROMOTING COMPLEX SUBUNIT 10
M: ANAPHASE-PROMOTING COMPLEX SUBUNIT 13
N: ANAPHASE-PROMOTING COMPLEX SUBUNIT 2
O: ANAPHASE-PROMOTING COMPLEX SUBUNIT 5
P: CELL DIVISION CYCLE PROTEIN 23 HOMOLOG
R: CELL DIVISION CYCLE PROTEIN 20 HOMOLOG
S: PROBABLE SERINE/THREONINE-PROTEIN KINASE HSL1
W: ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26
X: ANAPHASE-PROMOTING COMPLEX SUBUNIT 7
Y: ANAPHASE-PROMOTING COMPLEX SUBUNIT 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,250,91724
Polymers1,250,72121
Non-polymers1963
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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ANAPHASE-PROMOTING COMPLEX SUBUNIT ... , 11 types, 13 molecules ABDEGWILMNOXY

#1: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 1 / APC1 / CYCLOSOME SUBUNIT 1 / MITOTIC CHECKPOINT REGULATOR / TESTIS-SPECIFIC GENE 24 PROTEIN / APC1


Mass: 216725.469 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9H1A4
#2: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 11 / APC11 / CYCLOSOME SUBUNIT 11 / HEPATOCELLULAR CARCINOMA-ASSOCIATED RING FINGER PROTEIN / APC11


Mass: 9854.647 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9NYG5
#4: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 15 / APC15


Mass: 14286.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P60006
#5: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 16 / APC16 / CYCLOSOME SUBUNIT 16 / APC16


Mass: 11677.995 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q96DE5
#7: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26 / ANAPHASE-PROMOTING COMPLEX SUBUNIT 12 / APC12 / CELL DIVISION CYCLE PROTEIN 26 HOMOLOG / APC12


Mass: 9793.999 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q8NHZ8
#8: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 4 / APC4 / CYCLOSOME SUBUNIT 4 / APC4


Mass: 92219.227 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UJX5
#10: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 10 / APC10 / CYCLOSOME SUBUNIT 10 / APC10


Mass: 21124.949 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UM13
#11: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 13 / APC13 / CYCLOSOME SUBUNIT 13 / APC13


Mass: 8528.309 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9BS18
#12: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 2 / APC2 / CYCLOSOME SUBUNIT 2 / APC2


Mass: 93938.977 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UJX6
#13: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 5 / APC5 / CYCLOSOME SUBUNIT 5 / APC5


Mass: 85179.766 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UJX4
#16: Protein ANAPHASE-PROMOTING COMPLEX SUBUNIT 7 / APC7 / CYCLOSOME SUBUNIT 7 / APC7


Mass: 66929.367 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UJX3

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CELL DIVISION CYCLE PROTEIN ... , 4 types, 7 molecules CPFHJKR

#3: Protein CELL DIVISION CYCLE PROTEIN 23 HOMOLOG / ANAPHASE-PROMOTING COMPLEX SUBUNIT 8 / APC8 / CYCLOSOME SUBUNIT 8 / APC8


Mass: 68921.031 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9UJX2
#6: Protein CELL DIVISION CYCLE PROTEIN 27 HOMOLOG / ANAPHASE-PROMOTING COMPLEX SUBUNIT 3 / APC3 / CDC27 HOMOLOG / CDC27HS / H-NUC / APC3


Mass: 91973.125 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P30260
#9: Protein CELL DIVISION CYCLE PROTEIN 16 HOMOLOG / ANAPHASE-PROMOTING COMPLEX SUBUNIT 6 / APC6 / CDC16 HOMOLOG / CDC16HS / CYCLOSOME SUBUNIT 6 / APC6


Mass: 71747.516 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PF1, PU1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q13042
#14: Protein CELL DIVISION CYCLE PROTEIN 20 HOMOLOG / P55CDC / CDC20


Mass: 54796.508 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: MODIFIED PFASTBAC HTA / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q12834

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Protein / Non-polymers , 2 types, 4 molecules S

#15: Protein PROBABLE SERINE/THREONINE-PROTEIN KINASE HSL1 / HSL1


Mass: 23658.162 Da / Num. of mol.: 1 / Fragment: RESIDUES 667-872
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli)
References: UniProt: P34244, non-specific serine/threonine protein kinase
#17: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: RECOMBINANT APC-CDC20- HSL1 COMPLEX / Type: COMPLEX
Buffer solutionName: 20MM HEPES, 150MM NACL, 0. 5MM TCEP / pH: 8 / Details: 20MM HEPES, 150MM NACL, 0. 5MM TCEP
SpecimenConc.: 0.15 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: CARBON
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Details: LIQUID ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company
MicroscopyModel: FEI POLARA 300 / Date: Oct 30, 2015
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 78000 X / Calibrated magnification: 78000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm / Cs: 2 mm
Specimen holderTemperature: 100 K
Image recordingElectron dose: 27 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k)

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Processing

SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 179660 / Refinement type: HALF-MAPS REFINED INDEPENDENTLY / Symmetry type: POINT
RefinementHighest resolution: 3.9 Å
Refinement stepCycle: LAST / Highest resolution: 4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms65459 0 3 0 65462

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