Copper Binding and Oligomerization Studies of the Metal Resistance Determinant CrdA from .

Within this research, the CrdA protein from (CrdA), a putative copper-binding protein important for the survival of bacterium, was biophysically characterized in a solution, and its binding affinity toward copper was experimentally determined. Incubation of CrdA with Cu(II) ions favors the formation of the monomeric species in the solution. The modeled CrdA structure shows a conserved methionine-rich region, a potential binding site for Cu(I), as in the structures of similar copper-binding proteins, CopC and PcoC, from and from , respectively.