ArticleThe Journal of biological chemistry2010
Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 80 citations in OpenAlex.
- Systematic characterization of PBP2 as the primary siderophore recognizer inMicrobial genomics · 2026Article
- A landscape of metallophore synthesis and uptake potential of the genusNAR genomics and bioinformatics · 2025Article
- Pheno- and genotypic iron acquisition of non-aureus staphylococci: a scoping review of literature with a focus on bovine mastitis.Veterinary research · 2025Article
- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
- Forging the iron-net: Towards a quantitative understanding of microbial communities via siderophore-mediated interactions.Quantitative biology (Beijing, China) · 2025Article
- Enterobactin and salmochelin S4 inhibit the growth ofFrontiers in cellular and infection microbiology · 2025Article
- Decoding the regulatory networks ofFrontiers in cellular and infection microbiology · 2025Article
- Nasal commensals reduce Staphylococcus aureus proliferation by restricting siderophore availability.The ISME journal · 2024Article
- Immunoproteomic analysis of the serum IgG response to cell wall-associated proteins of Staphylococcus aureus strains belonging to CC97 and CC151.Veterinary research · 2023Article
- Differentiating the roles of Mycobacterium tuberculosis substrate binding proteins, FecB and FecB2, in iron uptake.PLoS pathogens · 2023Article
- Combined proteomic and transcriptomic analysis of the antimicrobial mechanism of tannic acid againstFrontiers in pharmacology · 2023Article
- Review
- In vivo growth of Staphylococcus lugdunensis is facilitated by the concerted function of heme and non-heme iron acquisition mechanisms.The Journal of biological chemistry · 2022Article
- The Role of Iron inFrontiers in cell and developmental biology · 2022Review
- Heme-Dependent Siderophore Utilization Promotes Iron-Restricted Growth of the Staphylococcus aureusJournal of bacteriology · 2021Article
- Small molecule natural products in human nasal/oral microbiota.Journal of industrial microbiology & biotechnology · 2021Review
- Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020Review
- Emergence of Ferrichelatase Activity in a Siderophore-Binding Protein Supports an Iron Shuttle in Bacteria.ACS central science · 2020Article
- The Staphylococcus aureus ArlRS two-component system regulates virulence factor expression through MgrA.Molecular microbiology · 2020Article
- Crystal Structure of the Siderophore Binding Protein BauB Bound to an Unusual 2:1 Complex Between Acinetobactin and Ferric Iron.Biochemistry · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Many organisms use sophisticated systems to acquire growth-limiting iron. Iron limitation is especially apparent in bacterial pathogens of mammalian hosts where free iron concentrations are physiologically negligible. A common strategy is to secrete low molecular weight iron chelators, termed siderophores, and express high affinity receptors for the siderophore-iron complex. Staphylococcus aureus, a widespread pathogen, produces two siderophores, staphyloferrin A (SA) and staphyloferrin B (SB). We have determined the crystal structure of the staphyloferrin B receptor, SirA, at high resolution in both the apo and Fe(III)-SB (FeSB)-bound forms. SirA, a member of the class III binding protein family of metal receptors, has N- and C-terminal domains, each composed of mainly a β-stranded core and α-helical periphery. The domains are bridged by a single α-helix and together form the FeSB binding site. SB coordinates Fe(III) through five oxygen atoms and one nitrogen atom in distorted octahedral geometry. SirA undergoes conformational change upon siderophore binding, largely securing two loops from the C-terminal domain to enclose FeSB with a low nanomolar dissociation constant. The staphyloferrin A receptor, HtsA, homologous to SirA, also encloses its cognate siderophore (FeSA); however, the largest conformational rearrangements involve a different region of the C-terminal domain. FeSB is uniquely situated in the binding pocket of SirA with few of the contacting residues being conserved with those of HtsA interacting with FeSA. Although both SirA and HtsA bind siderophores from the same α-hydroxycarboxylate class, the unique structural features of each receptor provides an explanation for their distinct specificity.
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