Bacterial Cu(+)-ATPases: models for molecular structure-function studies
Related Experiment Video
Updated: Mar 17, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
José M Argüello1, Sarju J Patel, Julia Quintana
1Department of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA 01609, USA. arguello@wpi.edu.
Abstract:
The early discovery of the human Cu(+)-ATPases and their link to Menkes and Wilson's diseases brought attention to the unique role of these transporters in copper homeostasis. The characterization of bacterial Cu(+)-ATPases has significantly furthered our understanding of the structure, selectivity and transport mechanism of these enzymes, as well as their interplay with other elements of Cu(+) distribution networks. This review focuses on the structural-functional insights that have emerged from studies of bacterial Cu(+)-ATPases at the molecular level and how these observations have contributed to drawing up a comprehensive picture of cellular copper homeostasis.
Related Concept Videos
ATP Driven Pumps III: V-type Pumps
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
ATP Synthase: Mechanism
Cytoskeletal Proteins in Bacteria
ATP Synthase: Structure
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...

