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A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc
release_vu7hljyywrgwnod5bgbelndnpi
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Jelena Habjanic,
Oliver Zerbe,
Eva Freisinger
Abstract
The NMR solution structure of a <italic>Pseudomonas</italic> metallothionein reveals a different binding capacity for Zn<sup>II</sup> and Cd<sup>II</sup> ions that results in two novel metal-cluster topologies. Replacement of a non-coordinating residue by histidine decreases the kinetic lability of the cluster. All three structures reported show an identical protein fold.
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