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• W2325130401 endingPage "8877" @default.
• W2325130401 startingPage "8866" @default.
• W2325130401 abstract "Near transporter (NEAT) domains of the iron-regulated surface determinant (Isd) proteins are essential for the import of nutritional heme from host animals to Gram-positive pathogens such as Staphylococcus aureus. The order of transfer of heme between NEAT domains occurs from IsdH to IsdA to IsdC, without any energy input despite the similarity of their three-dimensional structures. We measured the free energy of binding of heme and various metalloporphyrins to each NEAT domain and found that the affinity of heme and non-iron porphyrins for NEAT domains increased gradually in the same order as that for heme transfer. To gain insight into the atomistic mechanism for the differential affinities, we performed in silico molecular dynamics simulation and in vitro site-directed mutagenesis. The simulations revealed that the negatively charged residues that are abundant in the loop between strand β1b and the 310 helix of IsdH-NEAT3 destabilize the interaction with the propionate group of heme. The higher affinity of IsdC was in part attributed to the formation of a salt bridge between its unique residue, Glu88, and the conserved Arg100 upon binding to heme. In addition, we found that Phe130 of IsdC makes the β7−β8 hairpin less flexible in the ligand-free form, which serves to reduce the magnitude of the entropy loss on binding to heme. We confirmed that substitution of these key residues of IsdC decreased its affinity for heme. Furthermore, IsdC mutants, whose affinities for heme were lower than those of IsdA, transferred heme back to IsdA. Thus, NEAT domains have evolved the characteristic residues on the common structural scaffold such that they exhibit different affinities for heme, thus promoting the efficient transfer of heme." @default.
• W2325130401 created "2016-06-24" @default.
• W2325130401 creator A5006608170 @default.
• W2325130401 creator A5017695005 @default.
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• W2325130401 creator A5052407958 @default.
• W2325130401 creator A5072979871 @default.
• W2325130401 creator A5077947736 @default.
• W2325130401 date "2013-11-25" @default.
• W2325130401 modified "2023-09-30" @default.
• W2325130401 title "Heme Binding Mechanism of Structurally Similar Iron-Regulated Surface Determinant Near Transporter Domains of <i>Staphylococcus aureus</i> Exhibiting Different Affinities for Heme" @default.
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• W2325130401 doi "https://doi.org/10.1021/bi4008325" @default.
• W2325130401 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24245481" @default.
• W2325130401 hasPublicationYear "2013" @default.
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