Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain

Maeda, Masahiro; Hamada, Daizo; Hoshino, Masaru; Onda, Yayoi; Hase, Toshiharu; Goto, Yuji

doi:info:doi/10.1074/jbc.M112002200

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タイトル	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
著者	Maeda, Masahiro Maeda, Masahiro
	Hamada, Daizo Hamada, Daizo
	Hoshino, Masaru Hoshino, Masaru
	Onda, Yayoi Onda, Yayoi
	Hase, Toshiharu Hase, Toshiharu
	Goto, Yuji Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda, Toshiharu Hase and Yuji Goto. Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain. J. Biol. Chem. 2002; 277, 17101-17107. © the American Society for Biochemistry and Molecular Biology
抄録	Maize ferredoxin-NADP+reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP+ binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP+ binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP+ binding domain but a disordered FAD binding domain.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	277
号	19
開始ページ	17101
終了ページ	17107
刊行年月	2002-05
ISSN	1083351X
NCID	AA1202472X
DOI	info:doi/10.1074/jbc.M112002200
URL	http://hdl.handle.net/11094/71303
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.277(19) P.17101-P.17107
DC.title	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
DC.creator	Maeda, Masahiro
	Hamada, Daizo
	Hoshino, Masaru
	Onda, Yayoi
	Hase, Toshiharu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2002-05
DC.identifier	info:doi/10.1074/jbc.M112002200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71303
DC.description	This research was originally published in the Journal of Biological Chemistry. Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda, Toshiharu Hase and Yuji Goto. Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain. J. Biol. Chem. 2002; 277, 17101-17107. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Maize ferredoxin-NADP+reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP+ binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP+ binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP+ binding domain but a disordered FAD binding domain.
citation_title	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
citation_author	Maeda, Masahiro
	Hamada, Daizo
	Hoshino, Masaru
	Onda, Yayoi
	Hase, Toshiharu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2002-05
citation_journal_title	Journal of Biological Chemistry
citation_volume	277
citation_issue	19
citation_firstpage	17101
citation_lastpage	17107
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M112002200
citation_public_url	http://hdl.handle.net/11094/71303

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