High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases.

@article{Liu2005HighqualityHM,
  title={High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases.},
  author={Gaohua Liu and Zhao-hui Li and Yiwen Chiang and Thomas Acton and Gaetano T. Montelione and Diana Murray and Thomas Szyperski},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 6},
  pages={1597-608}
}
The structural biology of proteins mediating iron-sulfur (Fe-S) cluster assembly is central for understanding several important biological processes. Here we present the NMR structure of the 16-kDa protein YgdK from Escherichia coli, which shares 35% sequence identity with the E. coli protein SufE. The SufE X-ray crystal structure was solved in parallel with the YdgK NMR structure in the Northeast Structural Genomics (NESG) consortium. Both proteins are (1) key components for Fe-S metabolism… CONTINUE READING