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. 2004 Mar 1;378(Pt 2):293–297. doi: 10.1042/BJ20031669

A novel copper site in a cyanobacterial metallochaperone.

Gilles P M Borrelly 1, Claudia A Blindauer 1, Ralf Schmid 1, Clive S Butler 1, Chris E Cooper 1, Ian Harvey 1, Peter J Sadler 1, Nigel J Robinson 1
PMCID: PMC1223992  PMID: 14711369

Abstract

The thylakoid lumen of the cyanobacterium Synechocystis PCC 6803 is supplied with copper via two copper-transporting ATPases and a metallochaperone intermediary. We show that the copper site of this metallochaperone is unusual and consists of two cysteine residues and a histidine imidazole located on structurally dynamic loops. Substitution of this histidine residue enhances bacterial two-hybrid interaction with the cytosolic copper exporter, but not the copper importer, suggesting that the interacting surfaces are distinct, with implications for metal transfer.

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Selected References

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