The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket.

@article{Dickson2015TheSO,
  title={The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket.},
  author={Claire F. Dickson and David A Jacques and Robert T Clubb and J Mitchell Guss and David A. Gell},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2015},
  volume={71 Pt 6},
  pages={1295-306}
}
Staphylococcus aureus is a common and serious cause of infection in humans. The bacterium expresses a cell-surface receptor that binds to, and strips haem from, human haemoglobin (Hb). The binding interface has previously been identified; however, the structural changes that promote haem release from haemoglobin were unknown. Here, the structure of the receptor-Hb complex is reported at 2.6 Å resolution, which reveals a conformational change in the α-globin F helix that disrupts the haem-pocket… CONTINUE READING