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  • Title: The position of the ATP binding site on the (Ca2+ + Mg2+)-ATPase.
    Author: Gutierrez-Merino C, Munkonge F, Mata AM, East JM, Levinson BL, Napier RM, Lee AG.
    Journal: Biochim Biophys Acta; 1987 Feb 26; 897(2):207-16. PubMed ID: 2949777.
    Abstract:
    We present a convenient method to calculate the efficiency of fluorescence energy transfer in two-dimensional membrane systems. We apply it to the analysis of energy transfer between phospholipid molecules labelled with fluorescein and rhodamine groups, and of energy transfer in reconstituted membranes containing (Ca2+ + Mg2+)-ATPase purified from sarcoplasmic reticulum, with the ATPase labelled at the ATP binding site with fluorescein as donor, and rhodamine-labelled lipid as acceptor. The ATP binding site is found to be distant from the plane of the lipid/water interface of the membrane. It is suggested that the ATPase is present in the membrane as a dimer, with the two ATP binding sites in the dimer being close to the protein/protein interface. Addition of vanadate causes no change in quenching, suggesting that the ATP binding site does not move significantly with respect to the lipid/water interface in the E1-E2 conformational transition of the ATPase.
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