Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A

The structure and dynamics of the second domain of the human Menkes protein (MNK2), which is expressed in Escherichia coli, are analyzed by NMR in both the apo- and copper-loaded forms. The results are compared with metallochaperones and soluble domains of P-type ATPase in order to relate the primary structure to the occurrence of structural rearrangements upon copper binding.