Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function.
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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) ? 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 ? helices rotations, pistoning and scissoring have been detected and correlated to the segmental motions of HAMP and DHp domains of CpxA.
SUBMITTER: Duclert-Savatier N
PROVIDER: S-EPMC6264157 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
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