Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 15, Issue 4, Pages 387-393Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2005.06.005
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The sarcoplasmic reticulum Ca2+-ATPase (SERCA1a) belongs to the group of P-type ATPases, which actively transport inorganic cations across membranes at the expense of ATP hydrolysis. Three-dimensional structures of several transport intermediates of SERCA1a, stabilized by structural analogues of ATP and phosphoryl groups, are now available at atomic resolution. This has enabled the transport cycle of the protein to be described, including the coupling of Ca2+ occlusion and phosphorylation by ATP, and of proton counter-transport and dephosphorylation. From these structures, Ca2+-ATPase gradually emerges as a molecular mechanical device in which some of the transmembrane segments perform Ca2+ transport by piston-like movements and by the transmission of reciprocating movements that affect the chemical reactivity of the cytosolic globular domains.
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