Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.

@inproceedings{Dunkle2019StructuralEF,
  title={Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.},
  author={Jack A Dunkle and Michela Bruno and F Wayne Outten and Patrick A Frantom},
  year={2019}
}
SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe–S cluster assembly pathway. In Escherichia coli, this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically, this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five X-ray crystal structures of SufS including a new… CONTINUE READING