Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA.

@article{Drees2015DistinctFO,
  title={Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA.},
  author={Steffen Lorenz Drees and Dominik F Beyer and Christina Lenders-Lomscher and Mathias L{\"u}bben},
  journal={Molecular microbiology},
  year={2015},
  volume={97 3},
  pages={423-38}
}
P1 B -ATPases are among the most common resistance factors to metal-induced stress. Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. In bacteria, these domains are primarily associated with metal binding… CONTINUE READING
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