Cu(I)-transport ATPases. Molecular architecture, catalysis and adaptation to extreme environments

RECOULAT ANGELINI, ALVARO A.; PLACENTI, M. AGUEDA; MELIAN, NOELIA A.; SABECKIS, M. LURDES; NOELIA I. BURGARDT; GONZÁLEZ-LEBRERO, RODOLFO M.; ROMAN, ERNESTO A.; GONZALEZ FLECHA, F LUIS

Advances in Medicine and Biology

Nova Publishers

Año: 2021; p. 65 - 130

P-type ATPases constitutes alarge group of integral membrane proteins involved in the activetransport across the cell membrane coupled to the hydrolysis of ATP.Among them, the Cu(I)-ATPases are present in cells from all threedomains of life where, with the help of other transport proteins andsoluble chaperones, maintain intracellular copper(I) homeostasis.They share structural and functional features with all P-ATPases,including the formation of phosphorylated intermediates during thereaction cycle. In this chapter, we will analyze the structure,stability, adaptation to extreme environments and the catalyticmechanism of these α-helical membrane proteins. We review recentadvances, regarding experimental work and hybrid QM/MM moleculardynamics simulations. Also, we present toy-model simulations that aidin the understanding of the ATP hydrolysis and transport couplingmechanisms.p { text-indent: 0.64cm; margin-bottom: 0.25cm; direction: ltr; line-height: 115%; text-align: justify; orphans: 2; widows: 2; background: transparent }p.western { font-size: 11pt }p.cjk { font-size: 11pt }a:visited { color: #800080; text-decoration: underline }a:link { color: #0000ff; text-decoration: underline }