Key result
Surface modification using diethylpyrocarbonate with mass spectrometry identified 15 residues from the surface of sarcoplasmic reticulum Ca2+-pump ATPase, revealing conformational changes upon binding.
Mass spectrometry with diethylpyrocarbonate modification reveals specific conformational changes in the domains of sarcoplasmic reticulum Ca2+-ATPase upon substrate binding.
Advances SERCA structural insights in animals; leaves open translation to human cardiac Ca2+ handling disorders.
We have identified 15 residues from the surface of sarcoplasmic reticulum Ca(2+)-pump ATPase, by mass spectrometry using diethylpyrocarbonate modification. The reactivity of 9 residues remained high under all the conditions. The reactivity of Lys-515 at the nucleotide site was severely inhibited by ATP, whereas that of Lys-158 in the A-domain decreased by one-half and increased by five-fold in the presence of Ca(2+) and MgF(4), respectively. These are well explained by solvent accessibility, pK(a) and nearby hydrophobicity of the reactive atom on the basis of the atomic structure. However, the reactivity of 4 residues near the interface among A-, N- and P-domain suggested larger conformational changes of these domains in membrane upon binding of Ca(2+) (Lys-436), ATP (Lys-158) and MgF(4) (His-5, -190, Lys-436).
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Narumi et al. (2012) studied this question. Diethylpyrocarbonate modification was evaluated on Residue reactivity and conformational changes. Surface modification using diethylpyrocarbonate with mass spectrometry identified 15 residues from the surface of sarcoplasmic reticulum Ca2+-pump ATPase, revealing conformational changes upon binding.
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