Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies.

@article{Miyatake2000SensoryMO,
  title={Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies.},
  author={Hideyuki Miyatake and Masahiro Mukai and Sam Park and Shin-ichi Adachi and Kosuke Tamura and Hiro Nakamura and Kayako Nakamura and Takahiro Tsuchiya and Tetsutaro Iizuka and Yoshitsugu Shiro},
  journal={Journal of molecular biology},
  year={2000},
  volume={301 2},
  pages={415-31}
}
FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the two-component system, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to the O(2) levels. The crystal structure of the sensor domain of FixL (RmFixLH), which contains a heme (Fe-porphyrin) as a sensing site, was determined at 1.4 A resolution. Based on the structural and spectroscopic analyses, we propose the O(2) sensing mechanism that differs from the case proposed… CONTINUE READING

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