Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus
journal contribution
posted on 2023-05-17, 23:50 authored by Dickson, CF, Kumar, KK, Jacques, DA, Malmirchegini, GR, Spirig, T, Mackay, JP, Clubb, RT, Guss, JM, David GellDavid GellBackground: 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.
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Publication title
Journal of Biological ChemistryVolume
289Issue
10Pagination
6728-6738ISSN
0021-9258Department/School
Menzies Institute for Medical ResearchPublisher
Amer Soc Biochemistry Molecular Biology IncPlace of publication
9650 Rockville Pike, Bethesda, USA, Md, 20814-3996Rights statement
Copyright 2014 by The American Society for Biochemistry and Molecular Biology, Inc.Repository Status
- Open
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