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PMID:14711369
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Citation |
Borrelly, GP, Blindauer, CA, Schmid, R, Butler, CS, Cooper, CE, Harvey, I, Sadler, PJ and Robinson, NJ (2004) A novel copper site in a cyanobacterial metallochaperone. Biochem. J. 378:293-7 |
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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. |
Links |
PubMed PMC1223992 Online version:10.1042/BJ20031669 |
Keywords |
ATP-Binding Cassette Transporters; Adenosine Triphosphatases/metabolism; Amino Acid Substitution; Bacterial Proteins/metabolism; Binding Sites; Carrier Proteins/metabolism; Cation Transport Proteins/chemistry; Cation Transport Proteins/genetics; Cation Transport Proteins/metabolism; Copper/analysis; Copper/chemistry; Copper/metabolism; Cyanobacteria/chemistry; Cyanobacteria/metabolism; Cysteine/analysis; Ferredoxins/chemistry; Histidine/analysis; Histidine/chemistry; Ion Transport; Models, Molecular; Protein Folding |
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