Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar.

@article{Tajima2011LigandSD,
  title={Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar.},
  author={Hirotaka Tajima and Katsumi Imada and Mayuko Sakuma and F. Hattori and Toshifumi Nara and Naoki Kamo and Michio Homma and Ikuro Kawagishi},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 49},
  pages={42200-10}
}
Escherichia coli has closely related amino acid chemoreceptors with distinct ligand specificity, Tar for l-aspartate and Tsr for l-serine. Crystallography of the ligand-binding domain of Tar identified the residues interacting with aspartate, most of which are conserved in Tsr. However, swapping of the nonconserved residues between Tsr and Tar did not change ligand specificity. Analyses with chimeric receptors led us to hypothesize that distinct three-dimensional arrangements of the conserved… CONTINUE READING

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