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    Characterizing the conformational dynamics of metal-free PsaA using molecular dynamics simulations and electron paramagnetic resonance spectroscopy

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    Access Status
    Open access
    Authors
    Deplazes, Evelyne
    Begg, S.
    Van Wonderen, J.
    Campbell, R.
    Kobe, B.
    Paton, J.
    MacMillan, F.
    McDevitt, C.
    O'Mara, M.
    Date
    2015
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Deplazes, E. and Begg, S. and Van Wonderen, J. and Campbell, R. and Kobe, B. and Paton, J. and MacMillan, F. et al. 2015. Characterizing the conformational dynamics of metal-free PsaA using molecular dynamics simulations and electron paramagnetic resonance spectroscopy. Biophysical Chemistry. 207: pp. 51-60.
    Source Title
    Biophysical Chemistry
    DOI
    10.1016/j.bpc.2015.08.004
    ISSN
    0301-4622
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/38506
    Collection
    • Curtin Research Publications
    Abstract

    Prokaryotic metal-ion receptor proteins, or solute-binding proteins, facilitate the acquisition of metal ions from the extracellular environment. Pneumococcal surface antigen A (PsaA) is the primary Mn2+-recruiting protein of the human pathogen Streptococcus pneumoniae and is essential for its in vivo colonization and virulence. The recently reported high-resolution structures of metal-free and metal-bound PsaA have provided the first insights into the mechanism of PsaA-facilitated metal binding. However, the conformational dynamics of metal-free PsaA in solution remain unknown. Here, we use continuous wave electron paramagnetic resonance (EPR) spectroscopy and molecular dynamics (MD) simulations to study the relative flexibility of the structural domains in metal-free PsaA and its distribution of conformations in solution. The results show that the crystal structure of metal-free PsaA is a good representation of the dominant conformation in solution, but the protein also samples structurally distinct conformations that are not captured by the crystal structure. Further, these results suggest that the metal binding site is both larger and more solvent exposed than indicated by the metal-free crystal structure. Collectively, this study provides atomic-resolution insight into the conformational dynamics of PsaA prior to metal binding and lays the groundwork for future EPR and MD based studies of PsaA in solution.

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