Open AccessConformational sampling of CpxA: Connecting HAMP motions to the histidine kinase function
Author(s) -
Nathalie Duclert-Savatier,
Guillaume Bouvier,
Michaël Nilges,
Thérèse E. Malliavin
Publication year - 2018
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0207899
Subject(s) - hamp , histidine kinase , response regulator , histidine , biophysics , molecular dynamics , hamp domain , chemistry , biochemistry , crystallography , binding site , biology , enzyme , bacterial protein , computational chemistry , binding domain , hepcidin , gene , immunology , inflammation
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.