『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=123544EID:123544, Map:0, LastModified:2012年11月3日(土) 18:00:05, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[[学科長]/[徳島大学.工学部.生物工学科]], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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組織 (推奨): 1.徳島文理大学 [継承]
2.徳島大学.工学部.生物工学科.生物反応工学講座 [継承]
著者 (必須): 1. (英) Tsuge Hideaki (日) (読)
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2.川上 竜巳 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部])
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3.櫻庭 春彦
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4. (英) Ago Hideo (日) (読)
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5. (英) Miyano Masashi (日) (読)
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6. (英) Aki Kenji (日) (読)
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7. (英) Katunuma Nobuhiko (日) (読)
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8.大島 敏久 ([九州大学])
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題名 (必須): (英) Crystal Structure of a Novel FAD-, FMN-, and ATP-containing L-Proline Dehydrogenase Complex from Pyrococcus horikoshii  (日)    [継承]
副題 (任意):
要約 (任意): (英) Two novel types of dye-linked L-proline dehydrogenase complex (PDH1 and PDH2) were found in a hyperthermophilic archaeon, Pyrococcus horikoshii OT3. Here we report the first crystal structure of PDH1, which is a heterooctameric complex (alphabeta)4 containing three different cofactors: FAD, FMN, and ATP. The structure was determined by x-ray crystallography to a resolution of 2.86 angstroms. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, was similar to that of monomeric sarcosine oxidase. On the other hand, the alpha subunit possessed a unique structure composed of a classical dinucleotide fold domain with ATP, a central domain, an N-terminal domain, and a Cys-clustered domain. Serving as a third cofactor, FMN was located at the interface between the alpha and beta subunits in a novel configuration. The observed structure suggests that FAD and FMN are incorporated into an electron transfer system, with electrons passing from the former to the latter. The function of ATP is unknown, but it may play a regulatory role. Although the structure of the alpha subunit differs from that of the beta subunit, except for the presence of an analogous dinucleotide domain with a different cofactor, the structural characteristics of PDH1 suggest that each represents a divergent enzyme that arose from a common ancestral flavoenzyme and that they eventually formed a complex to gain a new function. The structural characteristics described here reveal the PDH1 complex to be a unique diflavin dehydrogenase containing a novel electron transfer system.  (日)    [継承]
キーワード (推奨): 1. (英) Adenosine Triphosphate (日) (読) [継承]
2. (英) Archaeal Proteins (日) (読) [継承]
3. (英) Crystallography, X-Ray (日) (読) [継承]
4. (英) Flavin Mononucleotide (日) (読) [継承]
5. (英) Flavin-Adenine Dinucleotide (日) (読) [継承]
6. (英) Models, Molecular (日) (読) [継承]
7. (英) Multienzyme Complexes (日) (読) [継承]
8. (英) Proline Oxidase (日) (読) [継承]
9. (英) Protein Structure, Quaternary (日) (読) [継承]
10. (英) Protein Subunits (日) (読) [継承]
11. (英) Pyrococcus horikoshii (日) (読) [継承]
発行所 (推奨): The American Society for Biochemistry and Molecular Biology [継承]
誌名 (必須): The Journal of Biological Chemistry ([The American Society for Biochemistry and Molecular Biology])
(pISSN: 0021-9258, eISSN: 1083-351X)

ISSN (任意): 0021-9258
ISSN: 0021-9258 (pISSN: 0021-9258, eISSN: 1083-351X)
Title: The Journal of biological chemistry
Title(ISO): J Biol Chem
Publisher: American Society for Biochemistry and Molecular Biology
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 280 [継承]
(必須): 35 [継承]
(必須): 31045 31049 [継承]
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年月日 (必須): 西暦 2005年 9月 初日 (平成 17年 9月 初日) [継承]
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DOI (任意): 10.1074/jbc.C500234200    (→Scopusで検索) [継承]
PMID (任意): 16027125    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.Affiliation: Institute for Health Sciences, Tokushima Bunri University, 180 Nishihama-bouji, Yamashiro-cho, Tokushima 770-8514, Japan. tsuge@tokushima.bunri-u.ac.jp  (日)    [継承]
2.(英) Article.DataBankList.DataBank.DataBankName: PDB  (日)    [継承]
3.(英) Article.DataBankList.DataBank.AccessionNumberList.AccessionNumber: 1Y56  (日)    [継承]
4.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
5.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Hideaki Tsuge, Ryushi Kawakami, Haruhiko Sakuraba, Hideo Ago, Masashi Miyano, Kenji Aki, Nobuhiko Katunuma and Toshihisa Ohshima : Crystal Structure of a Novel FAD-, FMN-, and ATP-containing L-Proline Dehydrogenase Complex from Pyrococcus horikoshii, The Journal of Biological Chemistry, Vol.280, No.35, 31045-31049, 2005.
欧文冊子 ● Hideaki Tsuge, Ryushi Kawakami, Haruhiko Sakuraba, Hideo Ago, Masashi Miyano, Kenji Aki, Nobuhiko Katunuma and Toshihisa Ohshima : Crystal Structure of a Novel FAD-, FMN-, and ATP-containing L-Proline Dehydrogenase Complex from Pyrococcus horikoshii, The Journal of Biological Chemistry, Vol.280, No.35, 31045-31049, 2005.

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