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

Emil Thomsen; Seán A. Thompson; Parker R. Stow; Maren Cukor; Gideon Grogan; Anne‐Kathrin Duhme‐Klair; Alison Butler

doi:10.1039/d5cc05103g

January 1, 2025Chemical Communications

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

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Key Points

YiuA exhibits unprecedented selectivity for the Fe(iii) complex of the mono-catechol siderophore.
The study highlights the binding affinity of YiuA for the Fe(iii)–(Rb MC)2 complex over ruckerbactin.
The findings indicate intricate molecular mechanisms governing iron acquisition in Yersinia ruckeri.
Understanding YiuA's selectivity could inform approaches to target iron uptake in pathogens.

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Implication

Yersinia ruckeri's binding protein YiuA demonstrates selectivity for Fe(iii)–mono-catechol siderophore, suggesting unique mechanisms for iron uptake.

Abstract

Yersinia ruckeri produces the tri-catechol siderophore ruckerbactin, Rb, yet its periplasmic binding protein YiuA has unprecedented selectivity for the 1 : 2 Fe( iii ) complex of the mono-catechol siderophore, Fe( iii )–(Rb MC ) 2 .

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Thomsen et al. (2025) studied this question.

synapsesocial.com/papers/68f3eb011cfc5ad53f290912 https://doi.org/10.1039/d5cc05103g

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

Key Points

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Implication

Abstract

Discussion

Cite This Study

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

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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