Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 15, Issue 1, Pages 47-59Publisher
SPRINGER
DOI: 10.1007/s00775-009-0595-4
Keywords
Copper; P-type ATPase; CopA; ATP7A; ATP7B
Funding
- National Institutes of Health [R01 DK071865]
- NRSA award [F32DK077429]
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [F32DK077429, R01DK071865] Funding Source: NIH RePORTER
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Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B play an essential role in human physiological function. Their primary function is to deliver copper to the secretory pathway and export excess copper from the cell for removal or further utilization. Cells employ Cu-ATPases in numerous physiological processes that include the biosynthesis of copper-dependent enzymes, lactation, and response to hypoxia. Biochemical studies of human Cu-ATPases and their orthologs have demonstrated that Cu-ATPases share many common structural and mechanistic characteristics with other members of the P-type ATPase family. Nevertheless, the Cu-ATPases have a unique coordinate environment for their ligands, copper and ATP, and additional domains that are required for sophisticated regulation of their intracellular localization and activity. Here, we review recent progress that has been made in understanding the structure of Cu-ATPases from the analysis of their individual domains and orthologs from microorganisms, and speculate about the implications of these findings for the function and regulation of human copper pumps.
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