1R1N

Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae

Summary for 1R1N

• Entry DOI: 10.2210/pdb1r1n/pdb
• Related: 1D91 1O7T
• Descriptor: Ferric-iron Binding Protein, OXO-IRON CLUSTER 1, OXO-IRON CLUSTER 2, ... (5 entities in total)
• Functional Keywords: iron binding protein
• Biological source: Neisseria gonorrhoeae
• Cellular location: Periplasm: P17259
• Total number of polymer chains: 9
• Total formula weight: 306444.49

Authors

Zhu, H.,Alexeev, D.,Hunter, D.J.,Campopiano, D.J.,Sadler, P.J. (deposition date: 2003-09-24, release date: 2004-03-09, Last modification date: 2024-12-25)

Primary citation

Zhu, H.,Alexeev, D.,Hunter, D.J.,Campopiano, D.J.,Sadler, P.J.
Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif.
Biochem.J., 376:35-41, 2003

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.

PubMed: 13129433
DOI: 10.1042/BJ20031283

Experimental method

X-RAY DIFFRACTION (1.74 Å)