Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter.

@article{Ran2007BismethionineLT,
  title={Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter.},
  author={Yanchao Ran and Hui Zhu and Mengyao Liu and Mari{\'a}n Fabian and John S Olson and Roman Aranda and George N. Phillips and David M. Dooley and Benfang Lei},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 43},
  pages={31380-8}
}
The surface protein Shp of Streptococcus pyogenes rapidly transfers its hemin to HtsA, the lipoprotein component of the HtsABC transporter, in a concerted two-step process with one kinetic phase. The structural basis and molecular mechanism of this hemin transfer have been explored by mutagenesis and truncation of Shp. The heme-binding domain of Shp is in the amino-terminal region and is functionally active by itself, although inclusion of the COOH-terminal domain speeds up the process… CONTINUE READING
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