Abstract
Metal ions play important roles in many chemical and biochemical processes, such as oxidation, oxygen transport, and electron transfer. The cellular trafficking of metal ions is controlled by a group of low molecular weight (6-10 kDa), cysteine-rich proteins (∼30%) referred to as metallothioneins (MTs). X-ray crystallography and NMR studies of fully cadmium-metallated human MTs revealed two distinct metal-binding clusters: N-terminal β domain Cd3(Cys)9 (residue 1-30) and C-terminal α domain Cd4(Cys)11 (residue 31-61), with metals tetrahedrally coordinated to the cysteinyl thiols.
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