Structure of the hemoglobin-isdh complex reveals the molecular basis of iron capture by staphylococcus aureus. Dickson, C., Kumar, K., Jacques, D., Malmirchegini, G., Spirig, T., Mackay, J., Clubb, R., Guss, J., & Gell, D. Journal of Biological Chemistry, 289(10):6728-6738, 2014. doi abstract bibtex 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.
@article{
title = {Structure of the hemoglobin-isdh complex reveals the molecular basis of iron capture by staphylococcus aureus},
type = {article},
year = {2014},
pages = {6728-6738},
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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.},
bibtype = {article},
author = {Dickson, C.F. and Kumar, K.K. and Jacques, D.A. and Malmirchegini, G.R. and Spirig, T. and Mackay, J.P. and Clubb, R.T. and Guss, J.M. and Gell, D.A.},
doi = {10.1074/jbc.M113.545566},
journal = {Journal of Biological Chemistry},
number = {10}
}
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