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The Gram-positive bacterium  Staphylococcus pseudintermedius  is a leading cause of canine bacterial pyoderma, resulting in worldwide morbidity in dogs.  S. pseudintermedius  also causes life-threatening human infections. Furthermore, methicillin-resistant  S. pseudintermedius  is emerging, resembling the human health threat of methicillin-resistant  Staphylococcus aureus . Therefore it is increasingly important to characterize targets for intervention strategies to counteract  S. pseudintermedius  infections. Here we used biophysical methods, mutagenesis, and X-ray crystallography, to define the ligand-binding properties and structure of SitA, an  S. pseudintermedius  surface lipoprotein. SitA was strongly and specifically stabilized by Mn 2+  and Zn 2+  ions. Crystal structures of SitA complexed with Mn 2+  and Zn 2+  revealed a canonical class III solute-binding protein with the metal cation bound in a cavity between N- and C-terminal lobes. Unexpectedly, one crystal contained both apo- and holo-forms of SitA, revealing a large side-chain reorientation of His 64 , and associated structural differences accompanying ligand binding. Such conformational changes may regulate fruitful engagement of the cognate ABC (ATP-binding cassette) transporter system (SitBC) required for metal uptake. These results provide the first detailed characterization and mechanistic insights for a potential therapeutic target of the major canine pathogen  S. pseudintermedius , and also shed light on homologous structures in related staphylococcal pathogens afflicting humans.

Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen Staphylococcus pseudintermedius