Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site

Fujiwara, Kazuko; Toma, Sachiko; Okamura, Kazuko; Motokawa, Yutaro; Nakagawa, Atushi; Taniguchi, Hisaaki

doi:https://doi.org/10.1074/jbc.M505010200

Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site

Fujiwara, Kazuko; Toma, Sachiko; Okamura, Kazuko et al.

Journal of Biological Chemistry, 2005, 280(39), 33645-33651

アクセス数:446件（2025-06-30 14:58 集計）

固定URL: https://hdl.handle.net/11094/73652

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タイトル	Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site
著者	NRID 1000020108880 1000020108880 著者名 Fujiwara, Kazuko
	NRID 1000040363535 1000040363535 著者名 Toma, Sachiko
	NRID 1000010108863 1000010108863 著者名 Okamura, Kazuko 著者の別表記 Ikeda, Kazuko
	NRID 1000040004585 1000040004585 著者名 Motokawa, Yutaro
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 著者名 Nakagawa, Atushi
	NRID 1000010257636 1000010257636 著者名 Taniguchi, Hisaaki
内容	This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Sachiko Toma, Kazuko Okamura-Ikeda, Yutaro Motokawa, Atsushi Nakagawa and Hisaaki Taniguchi. Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site. Journal of Biological Chemistry. 2005; 280, 33645-33651. © the American Society for Biochemistry and Molecular Biology.
抄録	Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of α-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 Å resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	280(39)
ページ	33645-33651
刊行年月	2005-09
言語	英語
ハンドルURL	https://hdl.handle.net/11094/73652
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M505010200
関連情報 (isIdenticalTo)	PMID 16043486
アクセス権	open access
権利情報	© the American Society for Biochemistry and Molecular Biology.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

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. 2005, 280(39), p. 33645-33651
DC.title	Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site
DC.creator	Fujiwara, Kazuko
	Toma, Sachiko
	Okamura, Kazuko
	Motokawa, Yutaro
	Nakagawa, Atushi
	Taniguchi, Hisaaki
DC.creator	Ikeda, Kazuko
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2005-09
DC.identifier	https://doi.org/10.1074/jbc.M505010200
DC.description	This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Sachiko Toma, Kazuko Okamura-Ikeda, Yutaro Motokawa, Atsushi Nakagawa and Hisaaki Taniguchi. Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site. Journal of Biological Chemistry. 2005; 280, 33645-33651. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of α-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 Å resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73652
citation_title	Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site
citation_author	Fujiwara, Kazuko
	Toma, Sachiko
	Okamura, Kazuko
	Motokawa, Yutaro
	Nakagawa, Atushi
	Taniguchi, Hisaaki
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2005-09
citation_journal_title	Journal of Biological Chemistry
citation_volume	280
citation_issue	39
citation_firstpage	33645
citation_lastpage	33651
citation_doi	https://doi.org/10.1074/jbc.M505010200
citation_pmid	16043486
citation_public_url	https://hdl.handle.net/11094/73652

Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site

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