5DMS

Mouse Polo-box domain and Emi2 (169-177)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Structural basis for recognition of Emi2 by Polo-like kinase 1 and development of peptidomimetics blocking oocyte maturation and fertilization.

Jia, J.L.Han, Y.H.Kim, H.C.Ahn, M.Kwon, J.W.Luo, Y.Gunasekaran, P.Lee, S.J.Lee, K.S.Bang, J.K.Kim, N.H.Namgoong, S.

(2015) Sci Rep 5: 14626-14626

  • DOI: https://doi.org/10.1038/srep14626
  • Primary Citation of Related Structures:  
    5DMS, 5DMV, 5DNJ

  • PubMed Abstract: 

    In a mammalian oocyte, completion of meiosis is suspended until fertilization by a sperm, and the cell cycle is arrested by a biochemical activity called cytostatic factor (CSF). Emi2 is one of the CSFs, and it maintains the protein level of maturation promoting factor (MPF) by inhibiting ubiquitin ligase anaphase promoting complex/cyclosome (APC/C). Degradation of Emi2 via ubiquitin-mediated proteolysis after fertilization requires phosphorylation by Polo-like kinase 1 (Plk1). Therefore, recognition and phosphorylation of Emi2 by Plk1 are crucial steps for cell cycle resumption, but the binding mode of Emi2 and Plk1 is poorly understood. Using biochemical assays and X-ray crystallography, we found that two phosphorylated threonines (Thr(152) and Thr(176)) in Emi2 are each responsible for the recruitment of one Plk1 molecule by binding to its C-terminal polo box domain (PBD). We also found that meiotic maturation and meiosis resumption via parthenogenetic activation were impaired when Emi2 interaction with Plk1-PBD was blocked by a peptidomimetic called 103-8. Because of the inherent promiscuity of kinase inhibitors, our results suggest that targeting PBD of Plk1 may be an effective strategy for the development of novel and specific contraceptive agents that block oocyte maturation and/or fertilization.


  • Organizational Affiliation

    Department of Animal Sciences, Chungbuk National University, Republic of Korea.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase PLK1
A, C
237Mus musculusMutation(s): 0 
Gene Names: Plk1Plk
EC: 2.7.11.21
UniProt & NIH Common Fund Data Resources
Find proteins for Q07832 (Mus musculus)
Explore Q07832 
Go to UniProtKB:  Q07832
IMPC:  MGI:97621
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ07832
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
F-box only protein 43
B, D
9Mus musculusMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q8CDI2 (Mus musculus)
Explore Q8CDI2 
Go to UniProtKB:  Q8CDI2
IMPC:  MGI:1926053
Entity Groups  
UniProt GroupQ8CDI2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
TPO
Query on TPO
B, D
L-PEPTIDE LINKINGC4 H10 N O6 PTHR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.198 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.82α = 90
b = 70.45β = 90.13
c = 59.15γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 2015-10-28 
  • Deposition Author(s): Namgoong, S.

Revision History  (Full details and data files)

  • Version 1.0: 2015-10-28
    Type: Initial release