2W85

Structure of Pex14 in complex with Pex19


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural Basis for Competitive Interactions of Pex14 with the Import Receptors Pex5 and Pex19.

Neufeld, C.Filipp, F.V.Simon, B.Neuhaus, A.Schueller, N.David, C.Kooshapur, H.Madl, T.Erdmann, R.Schliebs, W.Wilmanns, M.Sattler, M.

(2009) EMBO J 28: 745

  • DOI: https://doi.org/10.1038/emboj.2009.7
  • Primary Citation of Related Structures:  
    2W84, 2W85

  • PubMed Abstract: 

    Protein import into peroxisomes depends on a complex and dynamic network of protein-protein interactions. Pex14 is a central component of the peroxisomal import machinery and binds the soluble receptors Pex5 and Pex19, which have important function in the assembly of peroxisome matrix and membrane, respectively. We show that the N-terminal domain of Pex14, Pex14(N), adopts a three-helical fold. Pex5 and Pex19 ligand helices bind competitively to the same surface in Pex14(N) albeit with opposite directionality. The molecular recognition involves conserved aromatic side chains in the Pex5 WxxxF/Y motif and a newly identified F/YFxxxF sequence in Pex19. The Pex14-Pex5 complex structure reveals molecular details for a critical interaction in docking Pex5 to the peroxisomal membrane. We show that mutations of Pex14 residues located in the Pex5/Pex19 binding region disrupt Pex5 and/or Pex19 binding in vitro. The corresponding full-length Pex14 variants are impaired in peroxisomal membrane localisation in vivo, showing that the molecular interactions mediated by the N-terminal domain modulate peroxisomal targeting of Pex14.


  • Organizational Affiliation

    EMBL Heidelberg, Heidelberg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEROXISOMAL MEMBRANE ANCHOR PROTEIN PEX1470Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O75381 (Homo sapiens)
Explore O75381 
Go to UniProtKB:  O75381
PHAROS:  O75381
GTEx:  ENSG00000142655 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75381
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PEROXIN-1912Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P40855 (Homo sapiens)
Explore P40855 
Go to UniProtKB:  P40855
PHAROS:  P40855
GTEx:  ENSG00000162735 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP40855
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-02-17
    Type: Initial release
  • Version 1.1: 2013-05-08
    Changes: Derived calculations, Other, Refinement description, Structure summary, Version format compliance
  • Version 1.2: 2024-05-15
    Changes: Data collection, Database references, Other