The structure of trp RNA-binding attenuation protein

@article{Antson1995TheSO,
  title={The structure of trp RNA-binding attenuation protein},
  author={A. Antson and J. Otridge and A. Brzozowski and E. Dodson and G. Dodson and K. Wilson and T. Smith and Min Yang and T. Kurecki and P. Gollnick},
  journal={Nature},
  year={1995},
  volume={374},
  pages={693-700}
}
  • A. Antson, J. Otridge, +7 authors P. Gollnick
  • Published 1995
  • Biology, Computer Science, Medicine
  • Nature
  • The crystal structure of the trp RNA-binding attenuation protein of Bacillus subtilis solved at 1.8 Å resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit β-sheets to form a β-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent β-sheets in the β-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon… CONTINUE READING

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