9HRP

Structure of YIUA from Yersinia ruckeri with iron

Summary for 9HRP

• Entry DOI: 10.2210/pdb9hrp/pdb
• Related: 9hrj 9ht5 9if3
• Descriptor: Periplasmic substrate-binding transport protein, FE (III) ION (3 entities in total)
• Functional Keywords: ruckerbactin, yersinia, siderophore, metal binding protein
• Biological source: Yersinia ruckeri
• Total number of polymer chains: 4
• Total formula weight: 153300.72

Authors

Thompson, S.,Thomsen, E.,Duhme-Klair, A.,Butler, A.,Grogan, G. (deposition date: 2024-12-18, release date: 2025-11-05, Last modification date: 2025-11-19)

Primary citation

Thomsen, E.,Thompson, S.,Stow, P.R.,Cukor, M.,Grogan, G.,Duhme-Klair, A.K.,Butler, A.
Yersinia ruckeri YRB periplasmic binding protein YiuA selectively recognizes a Fe(III)-mono-catecholate siderophore.
Chem.Commun.(Camb.), 61:17653-17656, 2025

PubMed Abstract: The marine pathogen synthesizes the tri-catecholate siderophore ruckerbactin, Rb, (DHB-Arg-Ser), 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 and Rb, 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, Fe(III)-(Rb). 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).

PubMed: 41098114
DOI: 10.1039/d5cc05103g

Experimental method

X-RAY DIFFRACTION (2.32 Å)