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Download fileThe structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket
journal contribution
posted on 2023-05-18, 16:16 authored by Dickson, CF, Jacques, DA, Clubb, RT, Guss, JM, David GellDavid GellStaphylococcus 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 structure and alters the Hb quaternary interactions. These features suggest potential mechanisms by which the S. aureus Hb receptor induces haem release from Hb.
History
Publication title
Acta Crystallographica. Section D: Biological CrystallographyVolume
71Pagination
1295-1306ISSN
0907-4449Department/School
Tasmanian School of MedicinePublisher
Blackwell MunksgaardPlace of publication
DenmarkRights statement
Copyright International Union of CrystallographyRepository Status
- Open