Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis.

@article{Dago2012StructuralBO,
  title={Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis.},
  author={Angel Dago and Alexander Schug and Andrea Procaccini and James A. Hoch and Martin Weigt and Hendrik Szurmant},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 26},
  pages={E1733-42}
}
Signal transduction proteins such as bacterial sensor histidine kinases, designed to transition between multiple conformations, are often ruled by unstable transient interactions making structural characterization of all functional states difficult. This study explored the inactive and signal-activated conformational states of the two catalytic domains of sensor histidine kinases, HisKA and HATPase. Direct coupling analyses, a global statistical inference approach, was applied to >13,000 such… CONTINUE READING
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