1r1n

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

spinqualitylabelsall models 1r1n, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r1n is a 9 chain structure with sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.74Å Ligands: CN1, CNB, CNF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferric-binding protein

Proteopedia Page Contributors and Editors (what is this?)

OCA