Crystal Structure of LexA A Conformational Switch for Regulation of Self-Cleavage

@article{Luo2001CrystalSO,
  title={Crystal Structure of LexA A Conformational Switch for Regulation of Self-Cleavage},
  author={Yu Luo and Richard A Pfuetzner and Steve Mosimann and Mark Paetzel and Elizabeth A. Frey and Maia M. Cherney and Baek S. Kim and John W. Little and Natalie C. J. Strynadka},
  journal={Cell},
  year={2001},
  volume={106},
  pages={585-594}
}
LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the… CONTINUE READING

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