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Publication Abstract from PubMed

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 degrees C. The crystal structure of ferrichrome-free FhuD was determined via molecular replacement at 1.6 A 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.

Crystal structure of FhuD at 1.6 A resolution: a ferrichrome-binding protein from the animal and human pathogen Staphylococcus pseudintermedius.,Abate F, Cozzi R, Maritan M, Lo Surdo P, Maione D, Malito E, Bottomley MJ Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):214-9. doi:, 10.1107/S2053230X16002272. Epub 2016 Feb 19. PMID:26919525^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.