Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer.
Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P(1B)-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.
Singleton
Chloe
C
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK.
Le Brun
Nick E
NE
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000378:metabolism*; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D000079922:Copper Transport Proteins; D006706:Homeostasis; D006801:Humans; D056511:Metallochaperones; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015534:Trans-Activators / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
C474500:ATOX1 protein, human; C093341:ATX1 protein, S cerevisiae; D001426:Bacterial Proteins; D002352:Carrier Proteins; D027682:Cation Transport Proteins; C092379:CopZ protein, Enterococcus hirae; D000079922:Copper Transport Proteins; D056511:Metallochaperones; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D003300:Copper; D000251:Adenosine Triphosphatases