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Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
José M. Argüello
Heavy metal P1B-type ATPases play a critical role in cell survival by maintaining appropriate intracellular metal concentrations. Archaeoglobus fulgidus CopB is a member of this family that transports Cu(II) from the cytoplasm to the exterior of the cell using ATP as energy source. CopB has a 264 amino acid ATPBD (ATP-binding domain) that is essential for ATP binding and hydrolysis as well as ultimately transducing the energy to the transmembrane metal-binding site for metal occlusion and export. The relevant conformations of this domain during the different steps of the catalytic cycle are still under discussion. Through crystal structures of the …