title: The structural basis for coupling of Ca2+ transport to ATP hydrolysis by the sarcoplasmic reticulum Ca2+-ATPase.
abstract: Recently, a series of structure determinations has nearly completed a structural description of the transport cycle of the sarcoplasmic reticulum Ca(2+)-ATPase, especially those steps concerned with the phosphorylation by ATP and the dephosphorylation reaction. From these structures Ca(2+)-ATPase emerges as a molecular machine, where globular cytosolic domains and transmembrane helices work in concert like a mechanical pump, as can be vividly demonstrated in animated versions of the pump cycle. The structures show that both ATP phosphorylation and dephosphorylation at Asp351 take place as nucleophilic SN2 reactions, which are associated with Ca(2+) and H(+) occluded states, respectively. These transitory steps ensure efficient coupling between Ca(2+) transport and ATP hydrolysis.
authors.affiliation: Department of Biophysics, Institute of Physiology and Biophysics, University of Aarhus, DK-8000, Aarhus C, Denmark. jvm@biophys.au.dk
authors.forename: Jesper Vuust
authors.initials: JV
authors.lastname: Møller
authors.forename: Claus
authors.initials: C
authors.lastname: Olesen
authors.forename: Anne-Marie Lund
authors.initials: AM
authors.lastname: Jensen
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000737:chemistry* / Q000378:metabolism*; D004735:Energy Transfer; D010766:Phosphorylation; D011487:Protein Conformation
chemical_list: D000255:Adenosine Triphosphate; D000252:Calcium-Transporting ATPases; D002118:Calcium