Journal
BIOESSAYS
Volume 40, Issue 2, Pages -Publisher
WILEY
DOI: 10.1002/bies.201700197
Keywords
chemoreceptor; coiled coil; HAMP domain; histidine kinase; membrane receptors; transmembrane signaling; two-component signaling systems
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Funding
- Russian Science Foundation [16-15-00242]
- CEA(IBS)-HGF(FZJ) STC 5.1 specific agreement
- Russian Science Foundation [16-15-00242] Funding Source: Russian Science Foundation
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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 NpSRII:NpHtrII. 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.
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