Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif
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Date
2003Author
Zhu, Haizhong
Alexeev, Dmitriy
Hunter, Dominic JB
Campopiano, Dominic J
Sadler, Peter J
Metadata
Abstract
We report a set of three 1.8–1.9 Å resolution X-ray crystal structures
of Neisseria gonorrhoeae Fbp (ferric-ion binding protein):
(i) open-cleft apo-Fbp containing bound phosphate, (ii) opencleft
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.
Key words: bacterial transferrin, dityrosyl motif, iron-binding
protein, iron transport, oxo-iron cluster, X-ray crystallography.