Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain.

@article{Almog1998CrystalSO,
  title={Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain.},
  author={Orna Almog and Travis Gallagher and Maria Tordova and Jemima Hoskins and Peter Bryan and Gary L Gilliland},
  journal={Proteins},
  year={1998},
  volume={31 1},
  pages={21-32}
}
The three-dimensional structure of a subtilisin BPN' construct that was produced and folded without its prodomain shows the tertiary structure is nearly identical to the wild-type enzyme and not a folding intermediate. The subtilisin BPN' variant, Sbt70, was cloned and expressed in Escherichia coli without the prodomain, the 77-residue N-terminal domain that catalyzes the folding of the enzyme into its native tertiary structure. Sbt70 has the high-affinity calcium-binding loop, residues 75 to… CONTINUE READING

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