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A novel copper site in a cyanobacterial metallochaperone.


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.

SUBMITTER: Borrelly GP 

PROVIDER: S-EPMC1223992 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature

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A novel copper site in a cyanobacterial metallochaperone.

Borrelly Gilles P M GP   Blindauer Claudia A CA   Schmid Ralf R   Butler Clive S CS   Cooper Chris E CE   Harvey Ian I   Sadler Peter J PJ   Robinson Nigel J NJ  

The Biochemical journal 20040301 Pt 2


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 inte  ...[more]

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