Mutational Replacements at the “Glycine Hinge” of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue

Volume: 56, Issue: 29, Pages: 3850 - 3862
Published: Jul 14, 2017
Abstract
Bacterial chemoreceptors are dimeric membrane proteins that transmit signals from a periplasmic ligand-binding domain to the interior of the cells. The highly conserved cytoplasmic domain consists of a long hairpin that in the dimer forms a four-helix coiled-coil bundle. The central region of the bundle couples changes in helix packing that occur in the membrane proximal region to the signaling tip, controlling the activity of an associated...
Paper Details
Title
Mutational Replacements at the “Glycine Hinge” of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue
Published Date
Jul 14, 2017
Volume
56
Issue
29
Pages
3850 - 3862
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