5KHR

Model of human Anaphase-promoting complex/Cyclosome complex (APC15 deletion mutant) in complex with the E2 UBE2C/UBCH10 poised for ubiquitin ligation to substrate (APC/C-CDC20-substrate-UBE2C)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Cryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin Ligation.

Yamaguchi, M.VanderLinden, R.Weissmann, F.Qiao, R.Dube, P.Brown, N.G.Haselbach, D.Zhang, W.Sidhu, S.S.Peters, J.M.Stark, H.Schulman, B.A.

(2016) Mol Cell 63: 593-607

  • DOI: https://doi.org/10.1016/j.molcel.2016.07.003
  • Primary Citation of Related Structures:  
    5KHR, 5KHU

  • PubMed Abstract: 

    The mitotic checkpoint complex (MCC) coordinates proper chromosome biorientation on the spindle with ubiquitination activities of CDC20-activated anaphase-promoting complex/cyclosome (APC/C(CDC20)). APC/C(CDC20) and two E2s, UBE2C and UBE2S, catalyze ubiquitination through distinct architectures for linking ubiquitin (UB) to substrates and elongating polyUB chains, respectively. MCC, which contains a second molecule of CDC20, blocks APC/C(CDC20)-UBE2C-dependent ubiquitination of Securin and Cyclins, while differentially determining or inhibiting CDC20 ubiquitination to regulate spindle surveillance, checkpoint activation, and checkpoint termination. Here electron microscopy reveals conformational variation of APC/C(CDC20)-MCC underlying this multifaceted regulation. MCC binds APC/C-bound CDC20 to inhibit substrate access. However, rotation about the CDC20-MCC assembly and conformational variability of APC/C modulate UBE2C-catalyzed ubiquitination of MCC's CDC20 molecule. Access of UBE2C is limiting for subsequent polyubiquitination by UBE2S. We propose that conformational dynamics of APC/C(CDC20)-MCC modulate E2 activation and determine distinctive ubiquitination activities as part of a response mechanism ensuring accurate sister chromatid segregation.


  • Organizational Affiliation

    Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 11,944Homo sapiensMutation(s): 0 
Gene Names: ANAPC1TSG24
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Go to UniProtKB:  Q9H1A4
PHAROS:  Q9H1A4
GTEx:  ENSG00000153107 
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UniProt GroupQ9H1A4
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 1184Homo sapiensMutation(s): 0 
Gene Names: ANAPC11HSPC214
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Find proteins for Q9NYG5 (Homo sapiens)
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PHAROS:  Q9NYG5
GTEx:  ENSG00000141552 
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UniProt GroupQ9NYG5
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division cycle protein 23 homologC,
O [auth P]
597Homo sapiensMutation(s): 0 
Gene Names: CDC23ANAPC8
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Find proteins for Q9UJX2 (Homo sapiens)
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PHAROS:  Q9UJX2
GTEx:  ENSG00000094880 
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UniProt GroupQ9UJX2
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 16D [auth E]110Homo sapiensMutation(s): 0 
Gene Names: ANAPC16C10orf104CENP-27
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GTEx:  ENSG00000166295 
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UniProt GroupQ96DE5
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division cycle protein 27 homologE [auth F],
G [auth H]
824Homo sapiensMutation(s): 0 
Gene Names: CDC27ANAPC3D0S1430ED17S978E
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GTEx:  ENSG00000004897 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit CDC26F [auth G],
S [auth W]
85Homo sapiensMutation(s): 0 
Gene Names: CDC26ANAPC12C9orf17
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PHAROS:  Q8NHZ8
GTEx:  ENSG00000176386 
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UniProt GroupQ8NHZ8
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 4H [auth I]818Homo sapiensMutation(s): 0 
Gene Names: ANAPC4APC4
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PHAROS:  Q9UJX5
GTEx:  ENSG00000053900 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division cycle protein 16 homologI [auth J],
J [auth K]
620Homo sapiensMutation(s): 0 
Gene Names: CDC16ANAPC6
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Find proteins for Q13042 (Homo sapiens)
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PHAROS:  Q13042
GTEx:  ENSG00000130177 
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UniProt GroupQ13042
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 10K [auth L]185Homo sapiensMutation(s): 0 
Gene Names: ANAPC10APC10
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PHAROS:  Q9UM13
GTEx:  ENSG00000164162 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 13L [auth M]74Homo sapiensMutation(s): 0 
Gene Names: ANAPC13
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GTEx:  ENSG00000129055 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 2M [auth N]822Homo sapiensMutation(s): 2 
Gene Names: ANAPC2APC2KIAA1406
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GTEx:  ENSG00000176248 
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 5N [auth O]755Homo sapiensMutation(s): 2 
Gene Names: ANAPC5APC5
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GTEx:  ENSG00000089053 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
Ubiquitin-conjugating enzyme E2 CP [auth Q]190Homo sapiensMutation(s): 0 
Gene Names: UBE2CUBCH10
EC: 2.3.2.23 (PDB Primary Data), 2.3.2.24 (PDB Primary Data)
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GTEx:  ENSG00000175063 
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UniProt GroupO00762
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division cycle protein 20 homologQ [auth R]499Homo sapiensMutation(s): 0 
Gene Names: CDC20
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Find proteins for Q12834 (Homo sapiens)
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PHAROS:  Q12834
GTEx:  ENSG00000117399 
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UniProt GroupQ12834
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
HSL1 peptideR [auth S]33Saccharomyces cerevisiaeMutation(s): 0 
UniProt
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
Anaphase-promoting complex subunit 7T [auth X],
U [auth Y]
565Homo sapiensMutation(s): 0 
Gene Names: ANAPC7APC7
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PHAROS:  Q9UJX3
GTEx:  ENSG00000196510 
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UniProt GroupQ9UJX3
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 6.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-08-24
    Type: Initial release
  • Version 1.1: 2016-08-31
    Changes: Database references
  • Version 1.2: 2024-03-06
    Changes: Data collection, Database references