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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 71; no. 6; pp. 1295 - 1306
• Main Authors: Dickson, Claire F., Jacques, David A., Clubb, Robert T., Guss, J. Mitchell, Gell, David A.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.06.2015
• Subjects: alpha-Globins - chemistry; Antigens, Bacterial - chemistry; haemoglobin; Hemoglobins - chemistry; iron-regulated surface determinant; Models, Molecular; NEAT domain; Protein Conformation; Receptors, Cell Surface - chemistry; Research Papers; Staphylococcus aureus; Staphylococcus aureus - chemistry; iron-regulated surface determinant; NEAT domain; haemoglobin; Staphylococcus aureus
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S1399004715005817

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.