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Transmembrane Signal Transduction in Two‐Component Systems: Piston, Scissoring, or Helical Rotation?
Author(s) -
Gushchin Ivan,
Gordeliy Valentin
Publication year - 2018
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201700197
Subject(s) - histidine kinase , allosteric regulation , biophysics , transmembrane protein , phototaxis , transmembrane domain , signal transduction , histidine , piston (optics) , chemistry , biology , crystallography , physics , biochemistry , enzyme , genetics , receptor , optics , wavefront
Allosteric and transmembrane (TM) signaling are among the major questions of structural biology. Here, we review and discuss signal transduction in four‐helical TM bundles, focusing on histidine kinases and chemoreceptors found in two‐component systems. Previously, piston, scissors, and helical rotation have been proposed as the mechanisms of TM signaling. We discuss theoretically possible conformational changes and examine the available experimental data, including the recent crystallographic structures of nitrate/nitrite sensor histidine kinase NarQ and phototaxis system Np SRII: Np HtrII. We show that TM helices can flex at multiple points and argue that the various conformational changes are not mutually exclusive, and often are observed concomitantly, throughout the TM domain or in its part. The piston and scissoring motions are the most prominent motions in the structures, but more research is needed for definitive conclusions.