Publication Date:
2016-02-19
Description:
Staphylococcus pseudintermediusis a leading cause of disease in dogs, and zoonosis causes human infections. Methicillin-resistantS. pseudintermediusstrains are emerging, resembling the global health threat ofS. aureus. Therefore, it is increasingly important to characterize potential targets for intervention againstS. pseudintermedius. Here, FhuD, anS. pseudintermediussurface 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 determinedviamolecular 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 ofS. pseudintermedius.
Electronic ISSN:
2053-230X
Topics:
Biology
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Chemistry and Pharmacology
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Geosciences
,
Physics
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