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  • A natively unfolded toxin domain uses its receptor as a folding template
    Anderluh, Gregor, 1969- ; Gökce, Isa ; Lakey, Jeremy H.
    Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly involved in molecular interactions. The essential N-terminal ... translocation domains of colicin toxinsfrom Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain(CoIN-(1-90)), whieh binds to the C-terminal domain of ToIA (ToIA-(296421)), shows a disordered far-UV CD spectrum, no near-UV CD signal, and non-cooperative thermal unfolding. As expected, ToIA-(296-421) displays both secondary structure in far-LTV CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65 °C. CD spectra of the 1:1 eomplex show both increased secondary structure and colicin N-specific near-L1V CD signals. A new cooperative thermal transition at 35 °C is followed by the unchanged unfolding behavior of ToIA-(296-421). Fluorescence and surface plasmon resonance confirm that the new unfolding transition accompanies dissociation of CoIN-(1-90). Hence upon binding the disordered structure of CoIN-(1-90) converts to a cooperatively folded domain without altering the TolA-(296-421) structure.
    Vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 279, št. 21, 2004, str. 22002-22009)
    Vrsta gradiva - članek, sestavni del
    Leto - 2004
    Jezik - angleški
    COBISS.SI-ID - 17722329

vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 279, št. 21, 2004, str. 22002-22009)
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