Structural highlights
Function
FBP_NEIGO This protein may be a central component in the iron-acquisition system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif.,Zhu H, Alexeev D, Hunter DJ, Campopiano DJ, Sadler PJ Biochem J. 2003 Nov 15;376(Pt 1):35-41. PMID:13129433[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhu H, Alexeev D, Hunter DJ, Campopiano DJ, Sadler PJ. Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif. Biochem J. 2003 Nov 15;376(Pt 1):35-41. PMID:13129433 doi:10.1042/BJ20031283
