Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT.

@article{Edayathumangalam2013CrystalSO,
  title={Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT.},
  author={Raji S Edayathumangalam and Rui Fu Wu and Rom{\'a}n Garc{\'i}a and Yuguang Wang and Wei Wang and Cheryl A Kreinbring and Alicia Bach and Jingling Liao and Todd Stone and Thomas C. Terwilliger and Quyen Q. Hoang and Boris R. Belitsky and Gregory A. Petsko and Dagmar Ringe and Dali Liu},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 44},
  pages={
          17820-5
        }
}
Bacillus subtilis GabR is a transcription factor that regulates gamma-aminobutyric acid (GABA) metabolism. GabR is a member of the understudied MocR/GabR subfamily of the GntR family of transcription regulators. A typical MocR/GabR-type regulator is a chimeric protein containing a short N-terminal helix-turn-helix DNA-binding domain and a long C-terminal pyridoxal 5'-phosphate (PLP)-binding putative aminotransferase domain. In the presence of PLP and GABA, GabR activates the gabTD operon, which… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 20 REFERENCES

The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR

DM van Aalten, CC DiRusso, J Knudsen
  • EMBO J 20(8):2041–2050
  • 2001
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Winged helix proteins.

  • Current opinion in structural biology
  • 2000
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure

JF Kirsch
  • J Mol Biol
  • 1984
VIEW 12 EXCERPTS
HIGHLY INFLUENTIAL