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© Research
Publication : PloS one

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in PloS one - 29 Nov 2018

Duclert-Savatier N, Bouvier G, Nilges M, Malliavin TE

Link to Pubmed [PMID] – 30496238

PLoS ONE 2018;13(11):e0207899

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.

https://www.ncbi.nlm.nih.gov/pubmed/30496238