Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins.

@article{Lin2007CrystalSO,
  title={Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins.},
  author={Jinzhong Lin and Tao Zhou and Keqiong Ye and Jinfeng Wang},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 37},
  pages={14640-5}
}
MitoNEET is a protein of unknown function present in the mitochondrial membrane that was recently shown to bind specifically the antidiabetic drug pioglizatone. Here, we report the crystal structure of the soluble domain (residues 32-108) of human mitoNEET at 1.8-A resolution. The structure reveals an intertwined homodimer, and each subunit was observed to bind a [2Fe-2S] cluster. The [2Fe-2S] ligation pattern of three cysteines and one histidine differs from the known pattern of four cysteines… CONTINUE READING
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