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

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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 Gell
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.

History

Publication title

Journal of Biological Chemistry

Volume

289

Issue

10

Pagination

6728-6738

ISSN

0021-9258

Department/School

Menzies Institute for Medical Research

Publisher

Amer Soc Biochemistry Molecular Biology Inc

Place of publication

9650 Rockville Pike, Bethesda, USA, Md, 20814-3996

Rights statement

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

Repository Status

  • Open

Socio-economic Objectives

Expanding knowledge in the biological sciences

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