ArticleThe Journal of biological chemistry2010
The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket.
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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34 citing papers in PubMed, 79 citations in OpenAlex.
- 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
- Drug Susceptibility, Siderophore Production, and Genome Analysis ofAntibiotics (Basel, Switzerland) · 2025Article
- Bioinformatics and modelling studies of FhuD, the periplasmic siderophore binding protein from the plant pathogen Erwinia amylovora.PloS one · 2025Article
- Enterobactin and salmochelin S4 inhibit the growth ofFrontiers in cellular and infection microbiology · 2025Article
- Nasal commensals reduce Staphylococcus aureus proliferation by restricting siderophore availability.The ISME journal · 2024Article
- Siderophores as tools and treatments.npj antimicrobials and resistance · 2024Review
- Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection.Cell host & microbe · 2023Article
- Differentiating the roles of Mycobacterium tuberculosis substrate binding proteins, FecB and FecB2, in iron uptake.PLoS pathogens · 2023Article
- 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
- Heme-Dependent Siderophore Utilization Promotes Iron-Restricted Growth of the Staphylococcus aureusJournal of bacteriology · 2021Article
- Genetic Regulation of Metal Ion Homeostasis in Staphylococcus aureus.Trends in microbiology · 2020Review
- 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
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- Structure and Metal Binding Properties ofJournal of bacteriology · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Crystal Structure of the Siderophore Binding Protein BauB Bound to an Unusual 2:1 Complex Between Acinetobactin and Ferric Iron.Biochemistry · 2018Article
- Structure and dynamics of Type III periplasmic proteins VcFhuD and VcHutB reveal molecular basis of their distinctive ligand binding properties.Scientific reports · 2017Article
- Application of a Novel "Pan-Genome"-Based Strategy for Assigning RNAseq Transcript Reads to Staphylococcus aureus Strains.PloS one · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Staphylococcus aureus uses several efficient iron acquisition strategies to overcome iron limitation. Recently, the genetic locus encoding biosynthetic enzymes for the iron chelating molecule, staphyloferrin A (SA), was determined. S. aureus synthesizes and secretes SA into its environment to scavenge iron. The membrane-anchored ATP binding cassette-binding protein, HtsA, receives the ferric-chelate for import into the cell. Recently, we determined the apoHtsA crystal structure, the first siderophore receptor from gram-positive bacteria to be structurally characterized. Herein we present the x-ray crystal structure of the HtsA-ferric-SA complex. HtsA adopts a class III binding protein fold composed of separate N- and C-terminal domains bridged by a single alpha-helix. Recombinant HtsA can efficiently sequester ferric-SA from S. aureus culture supernatants where it is bound within the pocket formed between distinct N- and C-terminal domains. A basic patch composed mainly of six Arg residues contact the negatively charged siderophore, securing it within the pocket. The x-ray crystal structures from two different ligand-bound crystal forms were determined. The structures represent the first structural characterization of an endogenous alpha-hydroxycarboxylate-type siderophore-receptor complex. One structure is in an open form similar to apoHtsA, whereas the other is in a more closed conformation. The conformational change is highlighted by isolated movement of three loops within the C-terminal domain, a domain movement unique to known class III binding protein structures.
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