The calcium uptake reaction kinetics of isolated sarcoplasmic reticulum (SR) vesicles have previously been shown to be at least biphasic over a range of temperatures (26 to 10 degrees C) with a fast phase identified with the formation of E1 approximately P and calcium occlusion and a slow phase with Ca2+ translocation across the membrane and turnover of the Ca2+ ATPase ensemble. At "low" temperatures, namely 0 degrees C or lower, E1 approximately P formation is slowed and E1 approximately P is transiently trapped for at least several seconds, as indicated by the absence of the slow phase for 6 s or more. We now report that a reversible, temperature-induced structural transition occurs at about 2-3 degrees C for the isolated SR membrane. We have investigated the nature of this structural transition utilizing meridional and equatorial x-ray diffraction studies of the oriented SR membrane multilayers in the range of temperatures between 7.5 and -2 degrees C. The phase meridional (lamellar) diffraction has provided the profile structure for the SR membrane at the highest vs. lowest temperature at the same moderate resolution of 16-17 A while the equatorial diffraction has provided information on the average lipid chain packing in the SR membrane plane in the two cases. To identify the contribution of each membrane component in producing the differences between the profile structures at 7.5 and -2 degrees C, step-function models have been fitted to the moderate resolution electron density profiles. Lipid lateral phase separation may be responsible for inducing the structural change in the Ca2+ ATPase, thereby resulting in the slowing of E1 approximately P formation and the transient trapping of E1 approximately P at the "lower" temperatures
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