4AOM

MTIP and MyoA complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.94 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Regulation of the Plasmodium Motor Complex: Phosphorylation of Myosin a Tail Interacting Protein (Mtip) Loosens its Grip on Myoa

Douse, C.H.Green, J.L.Salgado, P.S.Simpson, P.J.Thomas, J.C.Holder, A.A.Tate, E.W.Cota, E.

(2012) J Biol Chem 287: 36968

  • DOI: https://doi.org/10.1074/jbc.M112.379842
  • Primary Citation of Related Structures:  
    4AOM

  • PubMed Abstract: 

    The interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an essential feature of the conserved molecular machinery required for gliding motility and cell invasion by apicomplexan parasites. Recent data indicate that MTIP Ser-107 and/or Ser-108 are targeted for intracellular phosphorylation. Using an optimized MyoA tail peptide to reconstitute the complex, we show that this region of MTIP is an interaction hotspot using x-ray crystallography and NMR, and S107E and S108E mutants were generated to mimic the effect of phosphorylation. NMR relaxation experiments and other biophysical measurements indicate that the S108E mutation serves to break the tight clamp around the MyoA tail, whereas S107E has a smaller but measurable impact. These data are consistent with physical interactions observed between recombinant MTIP and native MyoA from Plasmodium falciparum lysates. Taken together these data support the notion that the conserved interactions between MTIP and MyoA may be specifically modulated by this post-translational modification.


  • Organizational Affiliation

    Institute of Chemical Biology, Imperial College London, SW7 2AZ, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MYOSIN A TAIL DOMAIN INTERACTING PROTEIN146Plasmodium falciparumMutation(s): 0 
UniProt
Find proteins for Q8I4W8 (Plasmodium falciparum (isolate 3D7))
Explore Q8I4W8 
Go to UniProtKB:  Q8I4W8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8I4W8
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MYOSIN-AB [auth T]18Plasmodium falciparumMutation(s): 0 
UniProt
Find proteins for Q8IDR3 (Plasmodium falciparum (isolate 3D7))
Explore Q8IDR3 
Go to UniProtKB:  Q8IDR3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8IDR3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.94 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.179 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.264α = 90
b = 54.704β = 90
c = 75.024γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-09-05
    Type: Initial release
  • Version 1.1: 2012-11-07
    Changes: Database references
  • Version 1.2: 2013-11-13
    Changes: Database references, Structure summary
  • Version 1.3: 2017-07-05
    Changes: Data collection
  • Version 1.4: 2023-12-20
    Changes: Data collection, Database references, Other, Refinement description