5FLY

The FhuD protein from S.pseudintermedius

Summary for 5FLY

• Entry DOI: 10.2210/pdb5fly/pdb
• Descriptor: Ferrichrome ABC transporter substrate-binding protein, CADMIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: metal transport, staphylococcal disease, siderophore, transport, iron, class iii solute binding protein
• Biological source: Staphylococcus pseudintermedius
• Total number of polymer chains: 2
• Total formula weight: 66003.78

Authors

Malito, E. (deposition date: 2015-10-29, release date: 2015-12-02, Last modification date: 2024-01-10)

Primary citation

Abate, F.,Cozzi, R.,Maritan, M.,Lo Surdo, P.,Maione, D.,Malito, E.,Bottomley, M.J.
Crystal Structure of Fhud at 1.6 Angstrom Resolution: A Ferrichrome-Binding Protein from the Animal and Human Pathogen Staphylococcus Pseudintermedius
Acta Crystallogr.,Sect.F, 72:214-, 2016

PubMed 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.

PubMed: 26919525
DOI: 10.1107/S2053230X16002272

Experimental method

X-RAY DIFFRACTION (1.598 Å)