Structure of the hemoglobin-isdh complex reveals the molecular basis of iron capture by staphylococcus aureus

Dickson, CF; Kumar, KK; Jacques, DA; Malmirchegini, GR; Spirig, T; Mackay, JP; Clubb, RT; Guss, JM; Gell, DA

Structure of the hemoglobin-isdh complex reveals the molecular basis of iron capture by staphylococcus aureus

Dickson, CF Kumar, KK Jacques, DA

Malmirchegini, GR Spirig, T Mackay, JP Clubb, RT Guss, JM Gell, DA

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Publication Type:: Journal Article
Citation:: Journal of Biological Chemistry, 2014, 289 (10), pp. 6728 - 6738
Issue Date:: 2014-03-07

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Field	Value	Language
dc.contributor.author	Dickson, CF	en_US
dc.contributor.author	Kumar, KK	en_US
dc.contributor.author	Jacques, DA https://orcid.org/0000-0002-6426-4510	en_US
dc.contributor.author	Malmirchegini, GR	en_US
dc.contributor.author	Spirig, T	en_US
dc.contributor.author	Mackay, JP	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.issued	2014-03-07	en_US
dc.identifier.citation	Journal of Biological Chemistry, 2014, 289 (10), pp. 6728 - 6738	en_US
dc.identifier.issn	0021-9258	en_US
dc.identifier.uri	http://hdl.handle.net/10453/118822
dc.description.abstract	Background: IsdB and IsdH proteins from Staphylococcus aureus strip heme iron from human hemoglobin. Results: The IsdH·hemoglobin complex shows how globin-binding and heme-binding NEAT domains of IsdH cooperate to remove heme from both chains of hemoglobin. Conclusion: The supradomain architecture of IsdH confers activity by precisely positioning the heme acceptor domain. Significance: Multiple IsdH·hemoglobin interfaces may be targets for new antibiotics. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.	en_US
dc.relation.ispartof	Journal of Biological Chemistry	en_US
dc.relation.isbasedon	10.1074/jbc.M113.545566	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Staphylococcus aureus	en_US
dc.subject.mesh	Staphylococcal Infections	en_US
dc.subject.mesh	Iron	en_US
dc.subject.mesh	Heme	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	Crystallography, X-Ray	en_US
dc.subject.mesh	Protein Structure, Secondary	en_US
dc.subject.mesh	Protein Structure, Tertiary	en_US
dc.title	Structure of the hemoglobin-isdh complex reveals the molecular basis of iron capture by staphylococcus aureus	en_US
dc.type	Journal Article
utslib.citation.volume	10	en_US
utslib.citation.volume	289	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health 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	closed_access
pubs.issue	10	en_US
pubs.publication-status	Published	en_US
pubs.volume	289	en_US

Abstract:

Background: IsdB and IsdH proteins from Staphylococcus aureus strip heme iron from human hemoglobin. Results: The IsdH·hemoglobin complex shows how globin-binding and heme-binding NEAT domains of IsdH cooperate to remove heme from both chains of hemoglobin. Conclusion: The supradomain architecture of IsdH confers activity by precisely positioning the heme acceptor domain. Significance: Multiple IsdH·hemoglobin interfaces may be targets for new antibiotics. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/118822