Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.

@article{Vvodov2010CrystalSO,
  title={Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.},
  author={Jitka V{\'e}vodov{\'a} and Michael T. Gamble and Georg K{\"u}nze and Antonio Ariza and Eleanor J. Dodson and D Dafydd Jones and Keith S Wilson},
  journal={Structure},
  year={2010},
  volume={18 6},
  pages={744-55}
}
The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other… CONTINUE READING
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