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Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus

Citation

Dickson, CF and Kumar, KK and Jacques, DA and Malmirchegini, GR and Spirig, T and Mackay, JP and Clubb, RT and Guss, JM and Gell, DA, Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus, Journal of Biological Chemistry, 289, (10) pp. 6728-6738. ISSN 0021-9258 (2014) [Refereed Article]


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Copyright Statement

Copyright 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

DOI: doi:10.1074/jbc.M113.545566

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.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Structural Biology (incl. Macromolecular Modelling)
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Biological Sciences
Author:Dickson, CF (Miss Claire Dickson)
Author:Gell, DA (Dr David Gell)
ID Code:90658
Year Published:2014
Web of Science® Times Cited:19
Deposited By:Menzies Institute for Medical Research
Deposited On:2014-04-15
Last Modified:2017-11-06
Downloads:209 View Download Statistics

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