pubmed-article:2931429 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0205838 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
pubmed-article:2931429 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:2931429 | pubmed:issue | 21 | lld:pubmed |
pubmed-article:2931429 | pubmed:dateCreated | 1985-10-30 | lld:pubmed |
pubmed-article:2931429 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:2931429 | pubmed:language | eng | lld:pubmed |
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pubmed-article:2931429 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2931429 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2931429 | pubmed:month | Sep | lld:pubmed |
pubmed-article:2931429 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2931429 | pubmed:author | pubmed-author:MartonosiAA | lld:pubmed |
pubmed-article:2931429 | pubmed:author | pubmed-author:TaylorK AKA | lld:pubmed |
pubmed-article:2931429 | pubmed:author | pubmed-author:Ting-BeallH... | lld:pubmed |
pubmed-article:2931429 | pubmed:author | pubmed-author:DuxLL | lld:pubmed |
pubmed-article:2931429 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2931429 | pubmed:day | 25 | lld:pubmed |
pubmed-article:2931429 | pubmed:volume | 260 | lld:pubmed |
pubmed-article:2931429 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2931429 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2931429 | pubmed:pagination | 11730-43 | lld:pubmed |
pubmed-article:2931429 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:2931429 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:2931429 | pubmed:articleTitle | Crystallization of the Ca2+-ATPase of sarcoplasmic reticulum by calcium and lanthanide ions. | lld:pubmed |
pubmed-article:2931429 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2931429 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2931429 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2931429 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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