The SufE sulfur-acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes.

@article{GoldsmithFischman2004TheSS,
  title={The SufE sulfur-acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes.},
  author={Sharon Goldsmith-Fischman and Alexandre P. Kuzin and William Edstrom and Jordi Benach and Ritu Shastry and Rong Xiao and Thomas B. Acton and Barry Honig and Gaetano T. Montelione and John Francis Hunt},
  journal={Journal of molecular biology},
  year={2004},
  volume={344 2},
  pages={549-65}
}
The isc and suf operons in Escherichia coli represent alternative genetic systems optimized to mediate the essential metabolic process of iron-sulfur cluster (Fe-S) assembly under basal or oxidative-stress conditions, respectively. Some of the proteins in these two operons share strong sequence homology, e.g. the cysteine desulfurases IscS and SufS, and presumably play the same role in the oxygen-sensitive assembly process. However, other proteins in these operons share no significant homology… CONTINUE READING

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