Infrared spectroscopic characterization of the structural changes connected with the E1----E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum.

作者: J L Arrondo , H H Mantsch , N Mullner , S Pikula , A Martonosi

DOI: 10.1016/S0021-9258(18)48043-X

关键词: Calcium ATPaseProtein secondary structureVesicleVanadateFourier transform infrared spectroscopyCrystallographyBiochemistryEndoplasmic reticulumInfrared spectroscopyChemistryMembrane lipids

摘要: Abstract The Ca2+-transporting ATPase (EC 3.6.1.38) of sarcoplasmic reticulum alternates between several conformational states during ATP-dependent Ca2+ transport. E1 conformation is stabilized by 0.1 mM and the E2 vanadate in a Ca2+-free medium. Fourier transform infrared spectroscopy reveals significant differences two that indicate protein secondary structure. corresponding spectra can be interconverted reversibly changing concentration spectral changes appearance new alpha-helical substructure connected with E1----E2 conversion accompanied small beta-turns, while beta-sheet content remains essentially unchanged. There are also C = O stretching vibrations ester carbonyl groups phospholipids intact not observed under identical conditions isolated lipid dispersions. These observations imply an effect proteins on structure interfacial regions dependent state Ca2+-ATPase. CH2- CH3-stretching frequencies membrane lipids affected significantly transition. vesicles presence 20 suggest stabilization similar to except for behavior COO- phospholipid may reflect charge effects bound Ca2+.

参考文章(45)
S Varga, N Mullner, S Pikula, S Papp, K Varga, A Martonosi, Pressure effects on sarcoplasmic reticulum. Journal of Biological Chemistry. ,vol. 261, pp. 13943- 13956 ,(1986) , 10.1016/S0021-9258(18)66964-9
H Susi, [22] Infrared spectroscopy—Conformation Methods in Enzymology. ,vol. 26, pp. 455- 472 ,(1972) , 10.1016/S0076-6879(72)26024-4
G Meissner, D B Fein, D B Fein, M E Harder, M E Harder, G W Brady, G W Brady, Liquid diffraction analysis of sarcoplasmic reticulum. II. Solvent electron contrast variation. Biophysical Journal. ,vol. 37, pp. 637- 645 ,(1982) , 10.1016/S0006-3495(21)00383-0
Grant R. Bartlett, Phosphorus Assay in Column Chromatography Journal of Biological Chemistry. ,vol. 234, pp. 466- 468 ,(1959) , 10.1016/S0021-9258(18)70226-3
R W Williams, T J Beeler, Secondary structure of calsequestrin in solutions and in crystals as determined by Raman spectroscopy. Journal of Biological Chemistry. ,vol. 261, pp. 12408- 12413 ,(1986) , 10.1016/S0021-9258(18)67255-2
V Renugopalakrishnan, P M Horowitz, M J Glimcher, Structural studies of phosvitin in solution and in the solid state. Journal of Biological Chemistry. ,vol. 260, pp. 11406- 11413 ,(1985) , 10.1016/S0021-9258(17)39041-5
M. Cortijo, A. Alonso, J.C. Gomez-Fernandez, D. Chapman, Intrinsic protein-lipid interactions Journal of Molecular Biology. ,vol. 157, pp. 597- 618 ,(1982) , 10.1016/0022-2836(82)90501-0
L Dux, K A Taylor, H P Ting-Beall, A Martonosi, Crystallization of the Ca2+-ATPase of sarcoplasmic reticulum by calcium and lanthanide ions. Journal of Biological Chemistry. ,vol. 260, pp. 11730- 11743 ,(1985) , 10.1016/S0021-9258(17)39091-9