High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded -Barrel Fold
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High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded -Barrel Fold Agnieszka Dryla,‡ Bernd Hoffmann,†‡ Dieter Gelbmann, Carmen Giefing, Markus Hanner, Andreas Meinke, Annaliesa S. Anderson, Walter Koppensteiner, Robert Konrat, Alexander von Gabain, and Eszter Nagy* Intercell AG, Vienna Biocenter 6, A-1030 Vienna, Austria; Department of Biomolecular Structural Chemistry, University of Vienna, Vienna Biocenter 5, A-1030, Vienna, Austria; Biovertis AG, Vienna Biocenter 6, A-1030 Vienna, Austria; and Merck and Co. Incorporated, 440 Sumneytown Pike, WP16 100, Westpoint, Pennsylvania 19486
منابع مشابه
High-affinity binding of the staphylococcal HarA protein to haptoglobin and hemoglobin involves a domain with an antiparallel eight-stranded beta-barrel fold.
Iron scavenging from the host is essential for the growth of pathogenic bacteria. In this study, we further characterized two staphylococcal cell wall proteins previously shown to bind hemoproteins. HarA and IsdB harbor homologous ligand binding domains, the so called NEAT domain (for "near transporter") present in several surface proteins of gram-positive pathogens. Surface plasmon resonance m...
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The pathogen Staphylococcus aureus uses iron-regulated surface determinant (Isd) proteins to scavenge the essential nutrient iron from host hemoproteins. The IsdH protein (also known as HarA) is a receptor for hemoglobin (Hb), haptoglobin (Hp), and the Hb-Hp complex. It contains three NEAT (NEAr Transporter) domains: IsdH(N1), IsdH(N2), and IsdH(N3). Here we show that they have different functi...
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تاریخ انتشار 2006