Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions

@inproceedings{Shi2010StructuralBF,
  title={Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions},
  author={Rong Shi and Ariane Proteau and Magda Villarroya and Isma{\"i}l Moukadiri and Linhua Zhang and Jean-François Trempe and Allan Matte and M. Eugenia Armengod and Miroslaw Cygler},
  booktitle={PLoS biology},
  year={2010}
}
The cysteine desulfurase IscS is a highly conserved master enzyme initiating sulfur transfer via persulfide to a range of acceptor proteins involved in Fe-S cluster assembly, tRNA modifications, and sulfur-containing cofactor biosynthesis. Several IscS-interacting partners including IscU, a scaffold for Fe-S cluster assembly; TusA, the first member of a… CONTINUE READING