9hrp

Publication Abstract from PubMed

The marine pathogen Yersinia ruckeri synthesizes the tri-catecholate siderophore ruckerbactin, Rb, (DHB-(L)Arg-(L)Ser)(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).

Yersinia ruckeri YRB periplasmic binding protein YiuA selectively recognizes a Fe(III)-mono-catecholate siderophore.,Thomsen E, Thompson S, Stow PR, Cukor M, Grogan G, Duhme-Klair AK, Butler A Chem Commun (Camb). 2025 Oct 16. doi: 10.1039/d5cc05103g. PMID:41098114^[1]

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