Calcium and copper transport ATPases: analogies and diversities in transduction and signaling mechanisms.

ABSTRACT: The calcium transport ATPase and the copper transport ATPase are members of the P-ATPase family and retain an analogous catalytic mechanism for ATP utilization, including intermediate phosphoryl transfer to a conserved aspartyl residue, vectorial displacement of bound cation, and final hydrolytic cleavage of Pi. Both ATPases undergo protein conformational changes concomitant with catalytic events. Yet, the two ATPases are prototypes of different features with regard to transduction and signaling mechanisms. The calcium ATPase resides stably on membranes delimiting cellular compartments, acquires free Ca(2+) with high affinity on one side of the membrane, and releases the bound Ca(2+) on the other side of the membrane to yield a high free Ca(2+) gradient. These features are a basic requirem

SUBMITTER: Inesi G 

PROVIDER: S-EPMC3145875 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature