Metal-protein interactions: structure information from Ni(2+)-induced pseudocontact shifts in a native nonmetalloprotein.
Information about the structure of a native nonmetalloprotein was obtained from the pseudocontact shifts induced by a paramagnetic metal ion bound to the protein. The approach exploits the presence of metal binding sites on the surface of the protein. Using Escherichia coli thioredoxin as a model protein, we show that potential binding sites can be identified using the Cu(2+) ion, and that pseudocontact shifts induced by a Ni(2+) ion bound to one of these sites can provide valuable long-range structure information about the protein.
Jensen
Malene Ringkjøbing
MR
Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen Ø, Denmark.
Led
Jens J
JJ
D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D009532:Nickel / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013879:Thioredoxins / Q000737:chemistry*
D013879:Thioredoxins; D003300:Copper; D009532:Nickel