『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=262427EID:262427, Map:0, LastModified:2013年7月11日(木) 14:45:11, Operator:[松井 栄里], Avail:TRUE, Censor:0, Owner:[川上 竜巳], 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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著者 (必須): 1. (英) Sakuraba Haruhiko (日) (読)
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2. (英) Yoneda Kazunari (日) (読)
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3. (英) Satomura Takenori (日) (読)
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4.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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5. (英) Ohshima Toshihisa (日) (読)
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題名 (必須): (英) Structure of a D-tagatose 3-epimerase-related protein from the hyperthermophilic bacterium Thermotoga maritima.  (日)    [継承]
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要約 (任意): (英) The crystal structure of a D-tagatose 3-epimerase-related protein (TM0416p) encoded by the hypothetical open reading frame TM0416 in the genome of the hyperthermophilic bacterium Thermotoga maritima was determined at a resolution of 2.2 A. The asymmetric unit contained two homologous subunits and a dimer was generated by twofold symmetry. The main-chain coordinates of the enzyme monomer proved to be similar to those of D-tagatose 3-epimerase from Pseudomonas cichorii and D-psicose 3-epimerase from Agrobacterium tumefaciens; however, TM0416p exhibited a unique solvent-accessible substrate-binding pocket that reflected the absence of an alpha-helix that covers the active-site cleft in the two aforementioned ketohexose 3-epimerases. In addition, the residues responsible for creating a hydrophobic environment around the substrate in TM0416p differ entirely from those in the other two enzymes. Collectively, these findings suggest that the substrate specificity of TM0416p is likely to differ substantially from those of other D-tagatose 3-epimerase family enzymes.  (日)    [継承]
キーワード (推奨): 1. (英) Bacterial Proteins (日) (読) [継承]
2. (英) Carbohydrate Epimerases (日) (読) [継承]
3. (英) Catalytic Domain (日) (読) [継承]
4. (英) Crystallography, X-Ray (日) (読) [継承]
5. (英) Hexoses (日) (読) [継承]
6. (英) Protein Structure, Secondary (日) (読) [継承]
7. (英) Structural Homology, Protein (日) (読) [継承]
8. (英) Substrate Specificity (日) (読) [継承]
9. (英) Thermotoga maritima (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Acta Crystallographica. Section F, Structural Biology and Crystallization Communications ([国際結晶学連合])
(eISSN: 1744-3091)

ISSN (任意): 1744-3091
ISSN: 1744-3091 (eISSN: 1744-3091)
Title: Acta crystallographica. Section F, Structural biology and crystallization communications
Title(ISO): Acta Crystallogr Sect F Struct Biol Cryst Commun
Publisher: International Union of Crystallography
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 65 [継承]
(必須): Pt 3 [継承]
(必須): 199 203 [継承]
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年月日 (必須): 西暦 2009年 2月 14日 (平成 21年 2月 14日) [継承]
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DOI (任意): 10.1107/S1744309109002115    (→Scopusで検索) [継承]
PMID (任意): 19255464    (→Scopusで検索) [継承]
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WOS (任意): 000263773200002 [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1107/S1744309109002115  (日)    [継承]
2.(英) Article.Affiliation: Department of Applied Biological Science, Kagawa University, Ikenobe, Miki-cho, Kita-gun, Japan.  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) OtherID: PMC2650453  (日)    [継承]

標準的な表示

和文冊子 ● Haruhiko Sakuraba, Kazunari Yoneda, Takenori Satomura, Ryushi Kawakami and Toshihisa Ohshima : Structure of a D-tagatose 3-epimerase-related protein from the hyperthermophilic bacterium Thermotoga maritima., Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, Vol.65, No.Pt 3, 199-203, 2009.
欧文冊子 ● Haruhiko Sakuraba, Kazunari Yoneda, Takenori Satomura, Ryushi Kawakami and Toshihisa Ohshima : Structure of a D-tagatose 3-epimerase-related protein from the hyperthermophilic bacterium Thermotoga maritima., Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, Vol.65, No.Pt 3, 199-203, 2009.

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