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. 2001 Jul 15;357(Pt 2):545–549. doi: 10.1042/0264-6021:3570545

Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH).

H Mira 1, M Vilar 1, E Pérez-Payá 1, L Peñarrubia 1
PMCID: PMC1221983  PMID: 11439106

Abstract

The Arabidopsis thaliana copper chaperone (CCH) is a small copper binding protein involved in copper trafficking. When compared to homologues from other eukaryotes, CCH has two different domains; the conserved N-domain and the plant-exclusive C-domain, a C-terminal extension with an unusual amino-acid composition. In order to characterize this extra C-domain, the CCH protein, the N-domain and the C-domain were all expressed separately in heterologous systems. While the N-domain retained the copper chaperone and antioxidant properties described for the yeast Atx1 and human HAH1 counterparts, the C-domain displayed particular structural properties that would be necessary to optimize copper homoeostasis in plant cells where it could be responsible for the metallochaperone plant-exclusive intercellular transport. The whole CCH protein and the C-domain, but not the N-domain, displayed altered SDS/PAGE mobilities. CD spectroscopy showed that the N-domain fold is representative of an alpha/beta protein, while the C-domain adopts an extended conformation.

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Selected References

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