Key result
Fluorescence polarization and energy transfer studies combined with crystallographic data yielded a structural model of Ca2+-ATPase identifying binding sites and rigid/flexible regions.
This review provides a structural model of the Ca2+-ATPase in the sarcoplasmic reticulum, highlighting its rigid and flexible regions and binding sites.
Ca2+-ATPase transitions occur without major secondary structure changes and are lipid-modulated without specific interactions; leaves open SERCA regulation mechanisms in cardiac disease.
The ATP-dependent Ca2+ transport in sarcoplasmic reticulum involves transitions between several structural states of the Ca2(+)-ATPase, that occur without major changes in the secondary structure. The rates of these transitions are modulated by the lipid environment and by interactions between ATPase molecules. Although the Ca2(+)-ATPase restricts the rotational mobility of a population of lipids, there is no evidence for specific interaction of the Ca2(+)-ATPase with phospholipids. Fluorescence polarization and energy transfer (FET) studies, using site specific fluorescent indicators, combined with crystallographic, immunological and chemical modification data, yielded a structural model of Ca2(+)-ATPase in which the binding sites of Ca2+ and ATP are tentatively identified. The temperature dependence of FET between fluorophores attached to different regions of the ATPase indicates the existence of 'rigid' and 'flexible' regions within the molecule characterized, by different degrees of thermally induced structural fluctuations.
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Martonosi et al. (1990) conducted a review in Ca2+-ATPase structure and dynamics. Fluorescence polarization and energy transfer studies combined with crystallographic data yielded a structural model of Ca2+-ATPase identifying binding sites and rigid/flexible regions.
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