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• W2030111846 abstract "We have developed a stable analog for the ADP-insensitive phosphoenzyme intermediate with two occluded Ca²⁺ at the transport sites (<i>E</i>2PCa₂) of sarcoplasmic reticulum Ca²⁺-ATPase. This is normally a transient intermediate state during phosphoenzyme isomerization from the ADP-sensitive to ADP-insensitive form and Ca²⁺ deocclusion/release to the lumen; <i>E</i>1PCa₂ → <i>E</i>2PCa₂ → <i>E</i>2P + 2Ca²⁺. Stabilization was achieved by elongation of the Glu⁴⁰-Ser⁴⁸ loop linking the Actuator domain and M1 (1st transmembrane helix) with four glycine insertions at Gly⁴⁶/Lys⁴⁷ and by binding of beryllium fluoride (BeF<i>_x</i>) to the phosphorylation site of the Ca²⁺-bound ATPase (<i>E</i>1Ca₂). The complex <i>E</i>2Ca₂·BeF₃⁻ was also produced by lumenal Ca²⁺ binding to <i>E</i>2·BeF₃⁻ (<i>E</i>2P ground state analog) of the elongated linker mutant. The complex was stable for at least 1 week at 25 °C. Only BeF<i>_x</i>, but not AlF<i>_x</i> or MgF<i>_x</i>, produced the <i>E</i>2PCa₂ structural analog. Complex formation required binding of Mg²⁺, Mn²⁺, or Ca²⁺ at the catalytic Mg²⁺ site. Results reveal that the phosphorylation product <i>E</i>1PCa₂ and the <i>E</i>2P ground state (but not the transition states) become competent to produce the <i>E</i>2PCa₂ transient state during forward and reverse phosphoenzyme isomerization. Thus, isomerization and lumenal Ca²⁺ release processes are strictly coupled with the formation of the acylphosphate covalent bond at the catalytic site. Results also demonstrate the critical structural roles of the Glu⁴⁰-Ser⁴⁸ linker and of Mg²⁺ at the catalytic site in these processes." @default.
• W2030111846 created "2016-06-24" @default.
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• W2030111846 date "2010-08-01" @default.
• W2030111846 modified "2023-10-17" @default.
• W2030111846 title "Stable Structural Analog of Ca2+-ATPase ADP-insensitive Phosphoenzyme with Occluded Ca2+ Formed by Elongation of A-domain/M1′-linker and Beryllium Fluoride Binding" @default.
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• W2030111846 doi "https://doi.org/10.1074/jbc.m110.144535" @default.
• W2030111846 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2915690" @default.
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