Cu⁺-specific CopB transporter: Revising P_1B-type ATPase classification.

ABSTRACT: The copper-transporting P_1B-ATPases, which play a key role in cellular copper homeostasis, have been divided traditionally into two subfamilies, the P_1B-1-ATPases or CopAs and the P_1B-3-ATPases or CopBs. CopAs selectively export Cu⁺ whereas previous studies and bioinformatic analyses have suggested that CopBs are specific for Cu²⁺ export. Biochemical and spectroscopic characterization of Sphaerobacter thermophilus CopB (StCopB) show that, while it does bind Cu²⁺, the binding site is not the prototypical P_1B-ATPase transmembrane site and does not involve sulfur coordination as proposed previously. Most important, StCopB exhibits metal-stimulated ATPase activity in response to Cu⁺, bu

SUBMITTER: Purohit R 

PROVIDER: S-EPMC5834730 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature