Open AccessThe structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α‐globin haem pocket
Author(s) -
Dickson Claire F.,
Jacques David A.,
Clubb Robert T.,
Guss J. Mitchell,
Gell David A.
Publication year - 2015
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004715005817
Subject(s) - staphylococcus aureus , globin , receptor , heme , protein quaternary structure , chemistry , hemoglobin , conformational change , helix (gastropod) , biology , biophysics , biochemistry , microbiology and biotechnology , bacteria , genetics , protein subunit , gene , enzyme , ecology , snail
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.