Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A

Fujiwara, Kazuko; Maita, Nobuo; Hosaka, Harumi; Okamura-Ikeda, Kazuko; Nakagawa, Atushi; Taniguchi, Hisaaki

doi:info:doi/10.1074/jbc.M109.078717

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タイトル	Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
著者	Fujiwara, Kazuko Fujiwara, Kazuko
	Maita, Nobuo Maita, Nobuo
	Hosaka, Harumi Hosaka, Harumi
	Okamura-Ikeda, Kazuko Okamura-Ikeda, Kazuko
	Nakagawa, Atushi Nakagawa, Atushi
	Taniguchi, Hisaaki Taniguchi, Hisaaki
内容	This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Nobuo Maita, Harumi Hosaka, Kazuko Okamura-Ikeda, Atsushi Nakagawa Hisaaki Taniguchi. Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A. Journal of Biological Chemistry. 2010; 285, 9971-9980. © the American Society for Biochemistry and Molecular Biology.
抄録	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, LplAlipoyl-5-AMP and LplAoctyl-5-AMPapoHprotein 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.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	285
号	13
開始ページ	9971
終了ページ	9980
刊行年月	2010-03
ISSN	1083351X
pmid	20089862
NCID	AA1202441X
DOI	info:doi/10.1074/jbc.M109.078717
URL	http://hdl.handle.net/11094/73657
権利情報	© the American Society for Biochemistry and Molecular Biology.
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
dcmi資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry.285(13) P.38517-P.38523
DC.title	Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
DC.creator	Fujiwara, Kazuko
	Maita, Nobuo
	Hosaka, Harumi
	Okamura-Ikeda, Kazuko
	Nakagawa, Atushi
	Taniguchi, Hisaaki
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2010-03
DC.identifier	info:doi/10.1074/jbc.M109.078717
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/73657
DC.description	This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Nobuo Maita, Harumi Hosaka, Kazuko Okamura-Ikeda, Atsushi Nakagawa Hisaaki Taniguchi. Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A. Journal of Biological Chemistry. 2010; 285, 9971-9980. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	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, LplAlipoyl-5-AMP and LplAoctyl-5-AMPapoHprotein 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.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
citation_title	Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
citation_author	Fujiwara, Kazuko
	Maita, Nobuo
	Hosaka, Harumi
	Okamura-Ikeda, Kazuko
	Nakagawa, Atushi
	Taniguchi, Hisaaki
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2010-03
citation_journal_title	Journal of Biological Chemistry
citation_volume	285
citation_issue	13
citation_firstpage	9971
citation_lastpage	9980
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M109.078717
citation_pmid	20089862
citation_public_url	http://hdl.handle.net/11094/73657

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