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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

Citation

Dickson, CF and Jacques, DA and Clubb, RT and Guss, JM and Gell, DA, The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket, Acta Crystallographica. Section D: Biological Crystallography, 71 pp. 1295-1306. ISSN 0907-4449 (2015) [Refereed Article]


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Copyright International Union of Crystallography

DOI: doi:10.1107/S1399004715005817

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 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.

Item Details

Item Type:Refereed Article
Keywords:NEAT domain, Staphylococcus aureus, haemoglobin, iron-regulated surface determinant
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Structural Biology (incl. Macromolecular Modelling)
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Infectious Diseases
Author:Dickson, CF (Miss Claire Dickson)
Author:Gell, DA (Dr David Gell)
ID Code:106002
Year Published:2015
Web of Science® Times Cited:2
Deposited By:Medicine (Discipline)
Deposited On:2016-01-22
Last Modified:2017-11-06
Downloads:50 View Download Statistics

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