Yersinia ruckeri YRB periplasmic binding protein YiuA selectively recognizes a Fe(iii)-mono-catecholate siderophore

Abstract

The marine pathogen Yersinia ruckeri synthesizes the tri-catecholate siderophore ruckerbactin, Rb, (DHB-^LArg-^LSer)₃, to acquire iron during infection. Its biosynthetic gene cluster encodes a single periplasmic binding protein, RupB, which surprisingly does not bind Fe(III)–Rb nor the Fe(III) complexes of its hydrolysis products, the di- and mono-catecholate siderophores Rb_DC and Rb_MC, with biologically relevant affinities. Instead, the periplasmic binding protein YiuA, encoded in a different region of the chromosome, binds the 1 : 2 Fe(III) complex of the mono-catecholate Rb_MC, Fe(III)–(Rb_MC)₂. YiuA is the first periplasmic binding protein (PBP) to selectively recognize a mono-catecholate siderophore, the structural basis of which was illuminated through X-ray crystallography of YiuA bound to Fe(III)–(Rb_MC)₂.