Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones.

@article{Yao2006StructureOT,
  title={Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones.},
  author={Yong Yao and Maria A. Martinez-Yamout and Tobin J. Dickerson and Andrew P. Brogan and Peter E. Wright and H Jane Dyson},
  journal={Journal of molecular biology},
  year={2006},
  volume={355 2},
  pages={262-73}
}
The three-dimensional structure of a complex between the N-terminal domain of the quorum sensing protein SdiA of Escherichia coli and a candidate autoinducer N-octanoyl-L-homoserine lactone (C8-HSL) has been calculated in solution from NMR data. The SdiA-HSL system shows the "folding switch" behavior that has been seen for quorum-sensing factors produced by… CONTINUE READING