Mechanism of transmembrane signaling by sensor histidine kinases Article Swipe

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Response regulator Transmembrane protein Histidine kinase Cell biology Mechanism (biology) Transmembrane domain Regulator Signal transduction Two-component regulatory system Histidine Ligand (biochemistry) Escherichia coli Biology Chemistry Biophysics Bacteria Biochemistry Bacterial protein Receptor Genetics Physics Amino acid Gene Quantum mechanics Mutant

Ivan Gushchin , Igor Melnikov , Vitaly Polovinkin , Andrii Ishchenko , Anastasia Yuzhakova , Pavel Buslaev , Gleb Bourenkov , Sergei Grudinin , Ekaterina Round , Taras Balandin , Valentin Borshchevskiy , Dieter Willbold , Gordon A. Leonard , Georg Büldt , А. Н. Попов , Valentin Gordeliy ·

YOU? · · 2017 · Open Access · · DOI: https://doi.org/10.1126/science.aah6345 · OA: W2614245280

Bacterial sensing mechanism revealed 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