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Stable Structural Analog of Ca^<2+>-ATPase ADP-insensitive Phosphoenzyme with Occluded Ca^<2+> Formed by Elongation of A-domain/M1′-linker and Beryllium Fluoride Binding
https://asahikawa-med.repo.nii.ac.jp/records/4046
https://asahikawa-med.repo.nii.ac.jp/records/404684ec5cb1-c2c2-44bb-958e-fd3a6c7affa8
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
4540.pdf (1.8 MB)
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| Item type | 学術雑誌論文 / Journal Article_02(1) | |||||
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| 公開日 | 2012-05-17 | |||||
| タイトル | ||||||
| タイトル | Stable Structural Analog of Ca^<2+>-ATPase ADP-insensitive Phosphoenzyme with Occluded Ca^<2+> Formed by Elongation of A-domain/M1′-linker and Beryllium Fluoride Binding | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
大保, 貴嗣
× 大保, 貴嗣× Danko, Stefania× Yamasaki, Kazuo× Suzuki, Hiroshi |
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| 書誌情報 |
Journal of Biological Chemistry 巻 285, 号 32, p. 24538-24547, 発行日 2010-08-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | PISSN | |||||
| 収録物識別子 | 0021-9258 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1074/jbc.M110.144535 | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | We have developed a stable analog for the ADP-insensitive phosphoenzyme intermediate with two occluded Ca^<2+> at the transport sites (E2PCa_2) of sarcoplasmic reticulum Ca^<2+>-ATPase. This is normally a transient intermediate state during phosphoenzyme isomerization from the ADP-sensitive to ADP-insensitive form and Ca^<2+> deocclusion/release to the lumen; E1PCa_2 → E2PCa_2 → E2P + 2Ca^<2+>. Stabilization was achieved by elongation of the Glu^<40>-Ser^<48> loop linking the Actuator domain and M1 (1st transmembrane helix) with four glycine insertions at Gly^<46>/Lys^<47> and by binding of beryllium fluoride (BeFx) to the phosphorylation site of the Ca^<2+>-bound ATPase (E1Ca_2). The complex E2Ca_2·BeF_3− was also produced by lumenal Ca^<2+> binding to E2·BeF_3− (E2P ground state analog) of the elongated linker mutant. The complex was stable for at least 1 week at 25℃. Only BeFx, but not AlFx or MgFx, produced the E2PCa_2 structural analog. Complex formation required binding of Mg^<2+>, Mn^<2+>, or Ca^<2+> at the catalytic Mg^<2+> site. Results reveal that the phosphorylation product E1PCa_2 and the E2P ground state (but not the transition states) become competent to produce the E2PCa_2 transient state during forward and reverse phosphoenzyme isomerization. Thus, isomerization and lumenal Ca^<2+> 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 Glu^<40>-Ser^<48> linker and of Mg^<2+> at the catalytic site in these processes. | |||||
| 言語 | en | |||||
| 注記 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. | |||||
| 資源タイプ | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | text | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| フォーマット | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
| ID(XooNIps) | ||||||
| 値 | 20529842 | |||||
| 閲覧数(XooNIps) | ||||||
| 値 | 1025 | |||||
| ダウンロード数(XooNIps) | ||||||
| 値 | 822 | |||||
