Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus
journal contributionposted 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 Gell
Background: IsdB and IsdH proteins from Staphylococcus aureus strip heme iron from human hemoglobin. Results: The IsdHÂ·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 IsdHÂ·hemoglobin interfaces may be targets for new antibiotics. Â© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication titleJournal of Biological Chemistry
Department/SchoolMenzies Institute for Medical Research
PublisherAmer Soc Biochemistry Molecular Biology Inc
Place of publication9650 Rockville Pike, Bethesda, USA, Md, 20814-3996
Rights statementCopyright 2014 by The American Society for Biochemistry and Molecular Biology, Inc.