Proteins that transport heavy metals in micro-organisms and mammals share similarities in their sequences and structures.

These proteins provide an important focus for research, some being involved in bacterial resistance to toxic metals, such as lead and cadmium, while others are involved in inherited human syndromes, such as Wilson's and Menke's diseases [1].

A conserved domain has been found in a number of these heavy metal transport or detoxification proteins [2]. The domain, which has been termed Heavy-Metal-Associated (HMA), contains two conserved cysteines that are probably involved in metal binding.

Structure solution of the fourth HMA domain of the Menke's copper transporting ATPase shows a well-defined structure comprising a four-stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold [2]. This fold is common to other domains and is classified as "ferredoxin-like".

1. Wilson disease and Menkes disease: new handles on heavy-metal transport. Trends Genet. 10, 246-52
2. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat. Struct. Biol. 5, 47-54

Proteins that transport heavy metals in micro-organisms and mammals share similarities in their s
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