Crystal structure of activated CheY. Comparison with other activated receiver domains.

@article{Lee2001CrystalSO,
  title={Crystal structure of activated CheY. Comparison with other activated receiver domains.},
  author={S Y Lee and Ho Seung Cho and Jeffrey G. Pelton and Dong Yan and Edward A Berry and David E Wemmer},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 19},
  pages={16425-31}
}
The crystal structure of BeF(3)(-)-activated CheY, with manganese in the magnesium binding site, was determined at 2.4-A resolution. BeF(3)(-) bonds to Asp(57), the normal site of phosphorylation, forming a hydrogen bond and salt bridge with Thr(87) and Lys(109), respectively. The six coordination sites for manganese are satisfied by a fluorine of BeF(3)(-), the side chain oxygens of Asp(13) and Asp(57), the carbonyl oxygen of Asn(59), and two water molecules. All of the active site… CONTINUE READING