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

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posted on 2023-05-18, 16:16 authored by Dickson, CF, Jacques, DA, Clubb, RT, Guss, JM, David GellDavid Gell
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 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 Crystallography

Volume

71

Pagination

1295-1306

ISSN

0907-4449

Department/School

Tasmanian School of Medicine

Publisher

Blackwell Munksgaard

Place of publication

Denmark

Rights statement

Copyright International Union of Crystallography

Repository Status

  • Open

Socio-economic Objectives

Clinical health not elsewhere classified

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