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

Dickson, CF; Jacques, DA; Clubb, RT; Guss, JM; Gell, DA

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

Dickson, CF Jacques, DA

Clubb, RT Guss, JM Gell, DA

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Publication Type:: Journal Article
Citation:: Acta Crystallographica Section D: Biological Crystallography, 2015, 71 pp. 1295 - 1306
Issue Date:: 2015-06-01

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Field	Value	Language
dc.contributor.author	Dickson, CF	en_US
dc.contributor.author	Jacques, DA https://orcid.org/0000-0002-6426-4510	en_US
dc.contributor.author	Clubb, RT	en_US
dc.contributor.author	Guss, JM	en_US
dc.contributor.author	Gell, DA	en_US
dc.date.available	2015-03-23	en_US
dc.date.issued	2015-06-01	en_US
dc.identifier.citation	Acta Crystallographica Section D: Biological Crystallography, 2015, 71 pp. 1295 - 1306	en_US
dc.identifier.issn	0907-4449	en_US
dc.identifier.uri	http://hdl.handle.net/10453/119269
dc.description.abstract	© 2015 International Union of Crystallography. 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.	en_US
dc.relation.ispartof	Acta Crystallographica Section D: Biological Crystallography	en_US
dc.relation.isbasedon	10.1107/S1399004715005817	en_US
dc.subject.classification	Biophysics	en_US
dc.subject.mesh	Staphylococcus aureus	en_US
dc.subject.mesh	Hemoglobins	en_US
dc.subject.mesh	Receptors, Cell Surface	en_US
dc.subject.mesh	Antigens, Bacterial	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	alpha-Globins	en_US
dc.title	The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket	en_US
dc.type	Journal Article
utslib.citation.volume	71	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	02 Physical Sciences	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	open_access
pubs.publication-status	Published	en_US
pubs.volume	71	en_US

Abstract:

© 2015 International Union of Crystallography. 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.

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http://hdl.handle.net/10453/119269