ArticleThe Journal of biological chemistry2014
Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes.Scientific reports · 2024Article
- Effect of Three Bleaching Protocols on Tooth Discoloration Caused by Hemoglobin.Frontiers in dentistry · 2024Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Directed Inter-domain Motions Enable the IsdH Staphylococcus aureus Receptor to Rapidly Extract Heme from Human Hemoglobin.Journal of molecular biology · 2022Article
- Structure and role of the linker domain of the iron surface-determinant protein IsdH in heme transportation in Staphylococcus aureus.The Journal of biological chemistry · 2022Article
- Cryo-EM structures of staphylococcal IsdB bound to human hemoglobin reveal the process of heme extraction.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- The human protein haptoglobin inhibits IsdH-mediated heme-sequestering byThe Journal of biological chemistry · 2020Article
- The Staphylococcus aureus IsdH Receptor Forms a Dynamic Complex with Human Hemoglobin that Triggers Heme Release via Two Distinct Hot Spots.Journal of molecular biology · 2020Article
- NEAr Transporter (NEAT) Domains: Unique Surface Displayed Heme Chaperones That Enable Gram-Positive Bacteria to Capture Heme-Iron From Hemoglobin.Frontiers in microbiology · 2020Review
- Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.Scientific reports · 2019Article
- NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.Protein science : a publication of the Protein Society · 2019Article
- TheThe Journal of biological chemistry · 2018Article
- Energetics underlying hemin extraction from human hemoglobin byThe Journal of biological chemistry · 2018Article
- Structure-function analyses reveal key features inThe Journal of biological chemistry · 2018Article
- The Diversity of Mammalian Hemoproteins and Microbial Heme Scavengers Is Shaped by an Arms Race for Iron Piracy.Frontiers in immunology · 2018Article
- Expression, immunogenicity and variation of iron-regulated surface protein A from bovine isolates of Staphylococcus aureus.FEMS microbiology letters · 2017Article
- Molecular mechanisms of bio-catalysis of heme extraction from hemoglobin.Redox biology · 2017Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
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Abstract
Staphylococcus aureus causes life-threatening disease in humans. The S. aureus surface protein iron-regulated surface determinant H (IsdH) binds to mammalian hemoglobin (Hb) and extracts heme as a source of iron, which is an essential nutrient for the bacteria. However, the process of heme transfer from Hb is poorly understood. We have determined the structure of IsdH bound to human Hb by x-ray crystallography at 4.2 Å resolution, revealing the structural basis for heme transfer. One IsdH molecule is bound to each α and β Hb subunit, suggesting that the receptor acquires iron from both chains by a similar mechanism. Remarkably, two near iron transporter (NEAT) domains in IsdH perform very different functions. An N-terminal NEAT domain binds α/β globin through a site distant from the globin heme pocket and, via an intervening structural domain, positions the C-terminal heme-binding NEAT domain perfectly for heme transfer. These data, together with a 2.3 Å resolution crystal structure of the isolated N-terminal domain bound to Hb and small-angle x-ray scattering of free IsdH, reveal how multiple domains of IsdH cooperate to strip heme from Hb. Many bacterial pathogens obtain iron from human hemoglobin using proteins that contain multiple NEAT domains and other domains whose functions are poorly understood. Our results suggest that, rather than acting as isolated units, NEAT domains may be integrated into higher order architectures that employ multiple interaction interfaces to efficiently extract heme from host proteins.
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