Crystallization of the Ca2+-ATPase of Sarcoplasmic Reticulum by Calcium and Lanthanide Ions
Two-dimensional crystalline arrays of Ca2+-ATPase molecules develop in sarcoplasmic reticulum vesicles exposed to Ca2+ or lanthanide ions. The Ca2+- or lanthanide-induced crystals are presumed to represent the E1 conformation of the Ca2+-ATPase, and their crystal form is clearly different from the e...
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| Dokumentumtípus: | Cikk |
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1985
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| Sorozat: | JOURNAL OF BIOLOGICAL CHEMISTRY
260 No. 21 |
| Tárgyszavak: | |
| mtmt: | 1385323 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/26835 |
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| 024 | 7 | |a 1385323 |2 mtmt | |
| 040 | |a SZTE Publicatio Repozitórium |b hun | ||
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| 100 | 1 | |a Dux László | |
| 245 | 1 | 0 | |a Crystallization of the Ca2+-ATPase of Sarcoplasmic Reticulum by Calcium and Lanthanide Ions |h [elektronikus dokumentum] / |c Dux László |
| 260 | |c 1985 | ||
| 300 | |a 11730-11743 | ||
| 490 | 0 | |a JOURNAL OF BIOLOGICAL CHEMISTRY |v 260 No. 21 | |
| 520 | 3 | |a Two-dimensional crystalline arrays of Ca2+-ATPase molecules develop in sarcoplasmic reticulum vesicles exposed to Ca2+ or lanthanide ions. The Ca2+- or lanthanide-induced crystals are presumed to represent the E1 conformation of the Ca2+-ATPase, and their crystal form is clearly different from the earlier described E2 crystals induced by Na3VO4 in the presence of ethylene glycol bis(beta aminoethyl ether)-N,N,N',N'-tetraacetic acid (Taylor, K. A., Dux, L., and Martonosi, A. (1984) J. Mol. Biol. 174, 193-204). Analysis of the crystalline arrays by negative staining or freeze-fracture electron microscopy reveals obliquely oriented rows of particles corresponding to individual Ca2+-ATPase molecules. Computer analysis of the negatively stained lanthanide-induced crystalline Ca2+-ATPase arrays shows that the molecules are arranged in a P1 lattice. The pear-shaped profiles of Ca2+-ATPase molecules seen in projection in the density maps are similar to those seen in vanadate-induced crystals. The space group and unit cell dimensions of the E1 crystals are consistent with Ca2+-ATPase monomers as structural units, while the vanadate-induced E2 crystals form by lateral aggregation of chains of Ca2+-ATPase dimers. The transition between the E1 and E2 conformations may involve a shift in the monomer-oligomer equilibrium of the Ca2+-ATPase. The formation of E1 crystals by PrCl3 is promoted by inside negative membrane potential, presumably through stabilization of the E1 conformation of the enzyme. Cleavage of the Ca2+-ATPase by trypsin into two major fragments (A and B) did not interfere with the Ca2+- or the Pr3+-induced crystallization. | |
| 650 | 4 | |a Kémiai tudományok | |
| 700 | 0 | 1 | |a Taylor Kenneth A. |e aut |
| 700 | 0 | 2 | |a Ting-Beall H. Ping |e aut |
| 700 | 0 | 2 | |a Martonosi Anthony |e aut |
| 856 | 4 | 0 | |u http://publicatio.bibl.u-szeged.hu/26835/3/1385323.pdf |z Dokumentum-elérés |