A phenylalanine rotameric switch for signal-state control in bacterial chemoreceptors

Davi R. Ortega, Chen Yang, Peter Ames, Jerome Baudry (), John S. Parkinson and Igor B. Zhulin ()
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Davi R. Ortega: Joint Institute for Computational Sciences, University of Tennessee - Oak Ridge National Laboratory
Chen Yang: University of Utah
Peter Ames: University of Utah
Jerome Baudry: University of Tennessee
John S. Parkinson: University of Utah
Igor B. Zhulin: Joint Institute for Computational Sciences, University of Tennessee - Oak Ridge National Laboratory

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract Bacterial chemoreceptors are widely used as a model system for elucidating the molecular mechanisms of transmembrane signalling and have provided a detailed understanding of how ligand binding by the receptor modulates the activity of its associated kinase CheA. However, the mechanisms by which conformational signals move between signalling elements within a receptor dimer and how they control kinase activity remain unknown. Here, using long molecular dynamics simulations, we show that the kinase-activating cytoplasmic tip of the chemoreceptor fluctuates between two stable conformations in a signal-dependent manner. A highly conserved residue, Phe396, appears to serve as the conformational switch, because flipping of the stacked aromatic rings of an interacting F396-F396′ pair in the receptor homodimer takes place concomitantly with the signal-related conformational changes. We suggest that interacting aromatic residues, which are common stabilizers of protein tertiary structure, might serve as rotameric molecular switches in other biological processes as well.

Date: 2013
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DOI: 10.1038/ncomms3881

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