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- W2086406020 endingPage "348" @default.
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- W2086406020 abstract "Iron is an absolute requirement for nearly all organisms, but most bacterial pathogens are faced with extreme iron-restriction within their host environments. To overcome iron limitation pathogens have evolved precise mechanisms to steal iron from host supplies. Staphylococcus aureus employs the iron-responsive surface determinant (Isd) system as its primary heme–iron uptake pathway. Hemoglobin or hemoglobin–haptoglobin complexes are bound by Near iron-Transport (NEAT) domains within cell surface anchored proteins IsdB or IsdH. Heme is stripped from the host proteins and transferred between NEAT domains through IsdA and IsdC to the membrane transporter IsdEF for internalization. Once internalized, heme can be degraded by IsdG or IsdI, thereby liberating iron for the organism. Most components of the Isd system have been structurally characterized to provide insight into the mechanisms of heme binding and transport. This review summarizes recent research on the Isd system with a focus on the structural biology of heme recognition." @default.
- W2086406020 created "2016-06-24" @default.
- W2086406020 creator A5021302922 @default.
- W2086406020 creator A5036971247 @default.
- W2086406020 creator A5071277571 @default.
- W2086406020 creator A5087124975 @default.
- W2086406020 date "2010-03-01" @default.
- W2086406020 modified "2023-10-01" @default.
- W2086406020 title "Structural biology of heme binding in the Staphylococcus aureus Isd system" @default.
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- W2086406020 doi "https://doi.org/10.1016/j.jinorgbio.2009.09.012" @default.
- W2086406020 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19853304" @default.
- W2086406020 hasPublicationYear "2010" @default.
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