Download MendeleyOxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif.
Zhu, H., Alexeev, D., Hunter, D.J., Campopiano, D.J., Sadler, P.J.(2003) Biochem J 376: 35-41
- PubMed: 13129433
- DOI: https://doi.org/10.1042/BJ20031283
- Primary Citation of Related Structures:
1R1N - PubMed 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.
Organizational Affiliation:
School of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, Scotland, UK.
