1r1n
From Proteopedia
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Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae
Overview
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.
About this Structure
1R1N is a Single protein structure of sequence from Neisseria gonorrhoeae with CNB, CN1 and CNF as ligands. Full crystallographic information is available from OCA.
Reference
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
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