Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.

@article{Newberry2005CrystalSO,
  title={Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.},
  author={Kate J. Newberry and Shunji Nakano and Peter Zuber and Richard G Brennan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 44},
  pages={15839-44}
}
Spx, a global transcription regulator in Bacillus subtilis, interacts with the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase to control gene expression under conditions of disulfide stress, which is sensed by disulfide bond formation between Spx residues C10 and C13. Here, we describe the crystal structure of the B. subtilis alphaCTD bound to oxidized Spx. Analysis of the complex reveals interactions between three regions of "anti-alpha" Spx and helix alpha1 and the "261… CONTINUE READING

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Joint CCP4 ESF-EAMCB Newsletter on Protein Crystallography

A.G.W. Leslie
1992

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