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Mechanism of transmembrane signaling by sensor histidine kinases
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Journal Article
Mechanism of transmembrane signaling by sensor histidine kinases
2017
Overview
Escherichia coli use a transmembrane sensor protein to sense nitrate in their external environment and initiate a biochemical response. Gushchin et al. compared crystal structures of portions of the NarQ receptor that included the transmembrane helices in ligand-bound or unbound states. The structures suggest a signaling mechanism by which piston- and lever-like movements are transmitted to response regulator proteins within the cell. Such two-component systems are very common in bacteria and, if better understood, might provide targets for antimicrobial therapies. Science , this issue p. eaah6345 Crystal structures show how sensing of nitrate occurs in bacteria. One of the major and essential classes of transmembrane (TM) receptors, present in all domains of life, is sensor histidine kinases, parts of two-component signaling systems (TCSs). The structural mechanisms of TM signaling by these sensors are poorly understood. We present crystal structures of the periplasmic sensor domain, the TM domain, and the cytoplasmic HAMP domain of the Escherichia coli nitrate/nitrite sensor histidine kinase NarQ in the ligand-bound and mutated ligand-free states. The structures reveal that the ligand binding induces rearrangements and pistonlike shifts of TM helices. The HAMP domain protomers undergo leverlike motions and convert these pistonlike motions into helical rotations. Our findings provide the structural framework for complete understanding of TM TCS signaling and for development of antimicrobial treatments targeting TCSs.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science,American Association for the Advancement of Science (AAAS)
Subject
Antiinfectives and antibacterials
/ Bacteria
/ Binding
/ Biochemistry, Molecular Biology
/ Bonding
/ E coli
/ Escherichia coli - chemistry
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Helices
/ Kinases
/ Ligands
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Nitrates
/ Phosphoproteins - metabolism
/ Physics
/ Proteins
/ Segments
/ Sensors
/ Survival
/ Symmetry
