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Published in PLoS One - 11/13/2018
Nathalie Duclert-Savatier, Guillaume Bouvier, Michael Nilges, Thérèse E. Malliavin
. 2018; 13(11): e0207899.
Published online 2018 Nov 29. doi: 10.1371/journal.pone.0207899
PMCID: PMC6264157
PMID: 30496238


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.