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

Nathalie Duclert-Savatier (1) , Guillaume Bouvier (1) , Michael Nilges (1) , Thérèse Malliavin (1)

1 Bioinformatique structurale - Structural Bioinformatics

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.

Domains: Life Sciences [q-bio]; Biochemistry, Molecular Biology; Structural Biology [q-bio.BM]; Computer Science [cs]; Bioinformatics [q-bio.QM]; Life Sciences [q-bio]; Biochemistry, Molecular Biology; Biophysics

Nathalie Duclert-Savatier, Guillaume Bouvier, Michael Nilges, Thérèse Malliavin. Conformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function. PLoS ONE, 2018, 13 (11), pp.e0207899. ⟨10.1371/journal.pone.0207899⟩. ⟨pasteur-02330083⟩