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Proton nmr studies on nucleotide binding to the sarcoplasmic reticulum calcium atpase ec 3.6.1.3 determination of the conformations of bound nucleotides by the measurement of proton proton transferred nuclear overhauser enhancements



Proton nmr studies on nucleotide binding to the sarcoplasmic reticulum calcium atpase ec 3.6.1.3 determination of the conformations of bound nucleotides by the measurement of proton proton transferred nuclear overhauser enhancements



European Journal of Biochemistry 128(1): 113-118



The glycosidic bond torsion angles and the conformations of the ribose of Mg2+ ATP, Mg2+ ADP and Mg2+ AdoPP[NH]P (magnesium adenosine 5'-[.beta.,.gamma.-imido]triphosphate) bound to Ca2+ ATPase, both native and modified with fluorescein isothiocyanate (FITC), in intact [rabbit] sarcoplasmic reticulum were determined by the measurement of proton-proton transferred nuclear Overhauser enhancements by 1H-NMR spectroscopy. This method shows clearly the existence of a low-affinity ATP binding site after modification of the high-affinity site with FITC. For all 3 nucleotides bound to both the high-affinity (catalytic) site and the low-affinity site, the conformation about the glycosidic bond is anti, the conformation of the ribose 3'-endo of the N type and the conformation about the ribose C4'-C5' bond either gauche-trans or trans-gauche. The values for the glycosidic bond torsion angles .chi. (04'-C1'-N9-C4) for Mg2+ ATP, Mg2+ ADP and Mg2+ AdoPP[NH]P bound to the low-affinity site of FITC-modified Ca2+ ATPase are .apprxeq. 270.degree., .apprxeq. 260.degree. and .apprxeq. 240.degree., respectively. In the case of the nucleotides bound to the high-affinity (catalytic) site of native Ca2+ ATPase, .chi. lies in the range 240-280.degree.

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