Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.

@article{Roche2002MolecularDO,
  title={Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.},
  author={Philippe Roche and Liliane Mouawad and David P{\'e}rahia and J Samama and Daniel Kahn},
  journal={Protein science : a publication of the Protein Society},
  year={2002},
  volume={11 11},
  pages={2622-30}
}
FixJ is a two-domain response regulator involved in nitrogen fixation in Sinorhizobium meliloti. Recent X-ray characterization of both the native (unphosphorylated) and the active (phosphorylated) states of the protein identify conformational changes of the beta4-alpha4 loop and the conserved residue Phe101 as the key switches in activation. These structures also allowed investigation of the transition between conformations of this two-component regulatory receiver domain by molecular dynamics… CONTINUE READING