A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc
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The NMR solution structure of a Pseudomonas metallothionein reveals a different binding capacity for ZnII and CdII 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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2009 ◽
Vol 41
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pp. 343-348
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2014 ◽
Vol 188
(2)
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pp. 188-193
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2000 ◽
Vol 295
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pp. 1251-1264
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1997 ◽
Vol 267
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pp. 673-683
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1997 ◽
Vol 269
(3)
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pp. 408-422
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