Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture by Staphylococcus aureus. Dickson, C., F.; Kumar, K., K.; Jacques, D., A.; Malmirchegini, G., R.; Spirig, T.; Mackay, J., P.; Clubb, R., T.; Guss, J., M.; and Gell, D., A. Journal of Biological Chemistry, 289(10):6728-6738, 3, 2014.
Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture by Staphylococcus aureus [link]Website  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},
 identifiers = {[object Object]},
 pages = {6728-6738},
 volume = {289},
 websites = {http://www.jbc.org/lookup/doi/10.1074/jbc.M113.545566},
 month = {3},
 day = {7},
 id = {0ecd2a84-dbe2-3014-bf43-35960395eecc},
 created = {2020-10-01T06:20:37.895Z},
 file_attached = {false},
 profile_id = {45e2f77d-7a48-31e0-99de-4a07a154b051},
 group_id = {c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae},
 last_modified = {2020-10-29T21:44:44.525Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Dickson2014},
 source_type = {ARTICLE},
 notes = {cited By 22},
 private_publication = {false},
 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, Claire F. and Kumar, Kaavya Krishna and Jacques, David A. and Malmirchegini, G. Reza and Spirig, Thomas and Mackay, Joel P. and Clubb, Robert T. and Guss, J. Mitchell and Gell, David A.},
 journal = {Journal of Biological Chemistry},
 number = {10}
}
Downloads: 0