Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif
- 15 November 2003
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 376 (1) , 35-41
- https://doi.org/10.1042/bj20031283
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.Keywords
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