4XS0

Human methemoglobin in complex with the second and third NEAT domains of IsdH(F365Y/A369F/Y642A) from Staphylococcus aureus

Summary for 4XS0

• Entry DOI: 10.2210/pdb4xs0/pdb
• Related: 4IJ2
• Descriptor: Hemoglobin subunit alpha, Hemoglobin subunit beta, Iron-regulated surface determinant protein H, ... (7 entities in total)
• Functional Keywords: neat, heme/hemoglobin binding, hemoglobin, oxygen transport-protein binding complex, oxygen transport, metal transport
• Biological source: Staphylococcus aureus; More
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : Q2FG07
• Total number of polymer chains: 3
• Total formula weight: 71405.35

Authors

Dickson, C.F.,Jacques, D.A.,Guss, J.M.,Gell, D.A. (deposition date: 2015-01-21, release date: 2015-06-03, Last modification date: 2024-01-10)

Primary citation

Dickson, C.F.,Jacques, D.A.,Clubb, R.T.,Guss, J.M.,Gell, D.A.
The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native alpha-globin haem pocket.
Acta Crystallogr.,Sect.D, 71:1295-1306, 2015

PubMed Abstract: 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.

PubMed: 26057669
DOI: 10.1107/S1399004715005817

Experimental method

X-RAY DIFFRACTION (2.55 Å)