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Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function

Abstract : In the histidine kinase family, the HAMP and DHp domains are considered to play an important role into the transmission of signal arising from environmental conditions to the auto-phosphorylation site and to the binding site of response regulator. Several conformational motions inside HAMP have been proposed to transmit this signal: (i) the gearbox model, (ii) α helices rotations, pistons and scissoring, (iii) transition between ordered and disordered states. In the present work, we explore by temperature-accelerated molecular dynamics (TAMD), an enhanced sampling technique, the conformational space of the cytoplasmic region of histidine kinase CpxA. Several HAMP motions, corresponding to α helices rotations , pistoning and scissoring have been detected and correlated to the segmental motions of HAMP and DHp domains of CpxA.
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Nathalie Duclert-Savatier, Guillaume Bouvier, Michael Nilges, Thérèse Malliavin. Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function. PLoS ONE, Public Library of Science, 2018, 13 (11), pp.e0207899. ⟨10.1371/journal.pone.0207899⟩. ⟨pasteur-02330083⟩

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