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Global Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase A
https://tokushima-u.repo.nii.ac.jp/records/2012648
https://tokushima-u.repo.nii.ac.jp/records/20126485af3d650-99e2-4b4f-8ee6-b9af03e9fb67
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
jbc_285_13_9971.pdf (2.9 MB)
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| Item type | 文献 / Documents(1) | |||||||||||||||||||
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| 公開日 | 2025-03-07 | |||||||||||||||||||
| アクセス権 | ||||||||||||||||||||
| アクセス権 | open access | |||||||||||||||||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||||||||||||||||
| 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 | |||||||||||||||||||
| 出版社版DOI | ||||||||||||||||||||
| 関連識別子 | https://doi.org/10.1074/jbc.M109.078717 | |||||||||||||||||||
| 関連名称 | 10.1074/jbc.M109.078717 | |||||||||||||||||||
| 出版タイプ | ||||||||||||||||||||
| 出版タイプ | VoR | |||||||||||||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||||||||||||
| タイトル | ||||||||||||||||||||
| タイトル | Global Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase A | |||||||||||||||||||
| タイトル別表記 | ||||||||||||||||||||
| その他のタイトル | Conformational Changes of Lipoate-Protein Ligase A | |||||||||||||||||||
| 著者 |
Fujiwara, Kazuko
× Fujiwara, Kazuko
× 真板, 宣夫× Hosaka, Harumi
× Okamura-Ikeda, Kazuko
× Nakagawa, Atsushi
× 谷口, 寿章
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| 内容記述 | Lipoate-protein ligase A (LplA) catalyzes the attachment of lipoic acid to lipoate-dependent enzymes by a two-step reaction: first the lipoate adenylation reaction and, second, the lipoate transfer reaction. We previously determined the crystal structure of Escherichia coli LplA in its unliganded form and a binary complex with lipoic acid (Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A., and Taniguchi, H. (2005) J Biol. Chem. 280, 33645–33651). Here, we report two new LplA structures, LplA·lipoyl-5′-AMP and LplA·octyl-5′-AMP·apoH-protein complexes, which represent the post-lipoate adenylation intermediate state and the pre-lipoate transfer intermediate state, respectively. These structures demonstrate three large scale conformational changes upon completion of the lipoate adenylation reaction: movements of the adenylate-binding and lipoate-binding loops to maintain the lipoyl-5′-AMP reaction intermediate and rotation of the C-terminal domain by about 180°. These changes are prerequisites for LplA to accommodate apoprotein for the second reaction. The Lys133 residue plays essential roles in both lipoate adenylation and lipoate transfer reactions. Based on structural and kinetic data, we propose a reaction mechanism driven by conformational changes. | |||||||||||||||||||
| 書誌情報 |
en : Journal of Biological Chemistry 巻 285, 号 13, p. 9971-9980, 発行日 2010-01-19 |
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| 収録物識別子タイプ | EISSN | |||||||||||||||||||
| 収録物識別子 | 1083351X | |||||||||||||||||||
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| 収録物識別子タイプ | PISSN | |||||||||||||||||||
| 収録物識別子 | 00219258 | |||||||||||||||||||
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| 収録物識別子タイプ | NCID | |||||||||||||||||||
| 収録物識別子 | AA1202441X | |||||||||||||||||||
| 出版者 | ||||||||||||||||||||
| 出版者 | American Society for Biochemistry and Molecular Biology | |||||||||||||||||||
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| 出版者 | Elsevier | |||||||||||||||||||
| 権利情報 | ||||||||||||||||||||
| 権利情報 | This is an Open Access article under the CC BY license. | |||||||||||||||||||
| EID | ||||||||||||||||||||
| 識別子 | 207431 | |||||||||||||||||||
| 言語 | ||||||||||||||||||||
| 言語 | eng | |||||||||||||||||||
