Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions.

@article{Cobine2002CopperTF,
  title={Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions.},
  author={Paul A Cobine and Graham N George and Christopher E Jones and Wasantha A. Wickramasinghe and Marc Solioz and Charles T. Dameron},
  journal={Biochemistry},
  year={2002},
  volume={41 18},
  pages={5822-9}
}
Extracellular copper regulates the DNA binding activity of the CopY repressor of Enterococcus hirae and thereby controls expression of the copper homeostatic genes encoded by the cop operon. CopY has a CxCxxxxCxC metal binding motif. CopZ, a copper chaperone belonging to a family of metallochaperones characterized by a MxCxxC metal binding motif, transfers copper to CopY. The copper binding stoichiometries of CopZ and CopY were determined by in vitro metal reconstitutions. The stoichiometries… CONTINUE READING