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

Number of Access:592（2025-08-13 23:02 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73652

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Title	Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site
Creator	NRID 1000020108880 1000020108880 CreatorName Fujiwara, Kazuko
	NRID 1000040363535 1000040363535 CreatorName Toma, Sachiko
	NRID 1000010108863 1000010108863 CreatorName Okamura, Kazuko Creator.Alternative Ikeda, Kazuko
	NRID 1000040004585 1000040004585 CreatorName 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 CreatorName Nakagawa, Atushi
	NRID 1000010257636 1000010257636 CreatorName Taniguchi, Hisaaki
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.
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	280(39)
Page	33645-33651
Date of Issued	2005-09
Language	English
Handle URL	https://hdl.handle.net/11094/73652
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M505010200
Relation.isIdenticalTo	PMID 16043486
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. 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	English
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	English
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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