Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif

Haizhong Zhu, Dmitriy Alexeev, Dominic J B Hunter, Dominic J Campopiano, Peter J Sadler

Research output: Contribution to journalArticlepeer-review

Abstract

We report a set of three 1.8-1.9 A resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) open-cleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide 'snapshots' of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces.
Original languageEnglish
Pages (from-to)35-41
Number of pages7
JournalBiochemical Journal
Volume376
Issue numberPt 1
DOIs
Publication statusPublished - 2003

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