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

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

doi:https://doi.org/10.1074/jbc.M109.078717

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

Fujiwara, Kazuko; Maita, Nobuo; Hosaka, Harumi et al.

Journal of Biological Chemistry, 2010, 285(13), 9971-9980

Number of Access:709（2025-08-13 23:45 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73657

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Title	Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
Creator	NRID 1000020108880 1000020108880 CreatorName Fujiwara, Kazuko
	NRID 1000000404046 1000000404046 CreatorName Maita, Nobuo
	CreatorName Hosaka, Harumi
	NRID 1000010108863 1000010108863 CreatorName Okamura, Kazuko Creator.Alternative Ikeda, Kazuko
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 CreatorName Nakagawa, Atushi
	NRID 1000010257636 1000010257636 CreatorName Taniguchi, Hisaaki
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.
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	285(13)
Page	9971-9980
Date of Issued	2010-03
Language	English
Handle URL	https://hdl.handle.net/11094/73657
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M109.078717
Relation.isIdenticalTo	PMID 20089862
Access Rights	open access
CopyRight	© the American Society for Biochemistry and Molecular Biology.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2010, 285(13), p. 9971-9980
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, Kazuko
	Nakagawa, Atushi
	Taniguchi, Hisaaki
DC.creator	Ikeda, Kazuko
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2010-03
DC.identifier	https://doi.org/10.1074/jbc.M109.078717
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.
DC.format	73657
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, Kazuko
	Nakagawa, Atushi
	Taniguchi, Hisaaki
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2010-03
citation_journal_title	Journal of Biological Chemistry
citation_volume	285
citation_issue	13
citation_firstpage	9971
citation_lastpage	9980
citation_doi	https://doi.org/10.1074/jbc.M109.078717
citation_pmid	20089862
citation_public_url	https://hdl.handle.net/11094/73657

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

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