Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a Pb(II)/Zn(II)/Cd(II)-ATPase from Escherichia coli.

@article{Hou2001FunctionalAO,
  title={Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a Pb(II)/Zn(II)/Cd(II)-ATPase from Escherichia coli.},
  author={Zhanjun Hou and Suree Narindrasorasak and Bharat Bhushan and Biprajit Sarkar and B. B. d. Mitra},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 44},
  pages={
          40858-63
        }
}
ATP7B, the Wilson disease-associated Cu(I)-transporter, and ZntA from Escherichia coli are soft metal P1-type ATPases with mutually exclusive metal ion substrates. P1-type ATPases have a distinctive amino-terminal domain containing the conserved metal-binding motif GXXCXXC. ZntA has one copy of this motif while ATP7B has six copies. The effect of interchanging the amino-terminal domains of ATP7B and ZntA was investigated. Chimeric proteins were constructed in which either the entire amino… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 22 CITATIONS

Role of metal-binding domains of the copper pump from Archaeoglobus fulgidus.

  • Biochemical and biophysical research communications
  • 2006
VIEW 7 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Similar Papers

Loading similar papers…