Metal Selectivity of a Cd-, Co-, and Zn-Transporting P_1B-type ATPase.

ABSTRACT: The P_1B-ATPases, a family of transmembrane metal transporters important for transition metal homeostasis in all organisms, are subdivided into classes based on sequence conservation and metal specificity. The multifunctional P_1B-4-ATPase CzcP is part of the cobalt, zinc, and cadmium resistance system from the metal-tolerant, model organism Cupriavidus metallidurans. Previous work revealed the presence of an unusual soluble metal-binding domain (MBD) at the CzcP N-terminus, but the nature, extent, and selectivity of the transmembrane metal-binding site (MBS) of CzcP have not been resolved. Using homology modeling, we show that four wholly conserved amino acids from the transmembrane (TM) domain (Met²⁵⁴, Ser⁴⁷⁴, Cys⁴⁷⁶, and His^807</

SUBMITTER: Smith AT 

PROVIDER: S-EPMC5240476 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature