1r1n
Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeaeTri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae
Structural highlights
FunctionFBP_NEIGO This protein may be a central component in the iron-acquisition system. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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 AlsoReferences
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