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Crystal structure of FhuD at 1.6 Å resolution: a ferrichrome-binding protein from the animal and human pathogen
Francesca Abate1, Roberta Cozzi2, Martina Maritan2
1XBrane Biopharma, Stureplan 15, 111 45 Stockholm, Sweden.
Abstract:
Staphylococcus pseudintermedius is a leading cause of disease in dogs, and zoonosis causes human infections. Methicillin-resistant S. pseudintermedius strains are emerging, resembling the global health threat of S. aureus. Therefore, it is increasingly important to characterize potential targets for intervention against S. pseudintermedius. Here, FhuD, an S. pseudintermedius surface lipoprotein implicated in iron uptake, was characterized. It was found that FhuD bound ferrichrome in an iron-dependent manner, which increased the thermostability of FhuD by >15 °C. The crystal structure of ferrichrome-free FhuD was determined via molecular replacement at 1.6 Å resolution. FhuD exhibits the class III solute-binding protein (SBP) fold, with a ligand-binding cavity between the N- and C-terminal lobes, which is here occupied by a PEG molecule. The two lobes of FhuD were oriented in a closed conformation. These results provide the first detailed structural characterization of FhuD, a potential therapeutic target of S. pseudintermedius.
Insights
Researchers characterized FhuD, a surface lipoprotein in Staphylococcus pseudintermedius, crucial for iron uptake. Understanding FhuD
Area of Science:
- Veterinary microbiology
- Structural biology
- Protein biochemistry
Background:
- Staphylococcus pseudintermedius is a significant pathogen in dogs, with emerging methicillin-resistant strains posing a zoonotic risk.
- Characterizing potential therapeutic targets is crucial for combating S. pseudintermedius infections.
Purpose of the Study:
- To structurally characterize FhuD, an S. pseudintermedius surface lipoprotein involved in iron acquisition.
- To elucidate the structural basis of FhuD's interaction with its ligand.
Main Methods:
- Biochemical assays to determine ferrichrome binding and thermostability.
- X-ray crystallography to determine the high-resolution structure of FhuD.
- Molecular replacement for structure determination.
Main Results:
- FhuD binds ferrichrome in an iron-dependent manner, enhancing its thermostability by over 15 °C.
- The crystal structure of ferrichrome-free FhuD was determined at 1.6 Å resolution.
- FhuD displays a class III solute-binding protein fold with a closed conformation.
Conclusions:
- This study provides the first detailed structural characterization of FhuD.
- FhuD represents a potential therapeutic target for S. pseudintermedius infections.
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