Author
Listed:
- 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
Center for Molecular Biophysics, University of Tennessee - Oak Ridge National Laboratory)
- John S. Parkinson
(University of Utah)
- Igor B. Zhulin
(Joint Institute for Computational Sciences, University of Tennessee - Oak Ridge National Laboratory
University of Tennessee
Oak Ridge National Laboratory)
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.
Suggested Citation
Davi R. Ortega & Chen Yang & Peter Ames & Jerome Baudry & John S. Parkinson & Igor B. Zhulin, 2013.
"A phenylalanine rotameric switch for signal-state control in bacterial chemoreceptors,"
Nature Communications, Nature, vol. 4(1), pages 1-8, December.
Handle:
RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3881
DOI: 10.1038/ncomms3881
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