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Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine.

Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Research Abstract Details 

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  • Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Abstract Text:

    mitsuo kurataniMitsuo Kuratani,yuka yoshikawaYuka Yoshikawa,yoshitaka besshoYoshitaka Bessho,kyoko higashijimaKyoko Higashijima,takeshi ishiiTakeshi Ishii,rie shibataRie Shibata,seizo takahashiSeizo Takahashi,katsuhide yutaniKatsuhide Yutani,shigeyuki yokoyamaShigeyuki Yokoyama,mitsuo kurataniMitsuo Kuratani,yuka yoshikawaYuka Yoshikawa,yoshitaka besshoYoshitaka Bessho,kyoko higashijimaKyoko Higashijima,takeshi ishiiTakeshi Ishii,rie shibataRie Shibata,seizo takahashiSeizo Takahashi,katsuhide yutaniKatsuhide Yutani,shigeyuki yokoyamaShigeyuki Yokoyama,mitsuo kurataniMitsuo Kuratani,yuka yoshikawaYuka Yoshikawa,yoshitaka besshoYoshitaka Bessho,kyoko higashijimaKyoko Higashijima,takeshi ishiiTakeshi Ishii,rie shibataRie Shibata,seizo takahashiSeizo Takahashi,katsuhide yutaniKatsuhide Yutani,shigeyuki yokoyamaShigeyuki Yokoyama,

    In the bacterial genetic-code system, the codon AUA is decoded as isoleucine by tRNA(Ile)(2) with the lysidine residue at the wobble position. Lysidine is derived from cytidine, with ATP and L-lysine, by tRNA(Ile) lysidine synthetase (TilS), which is an N-type ATP pyrophosphatase. In this study, we determined the crystal structure of Aquifex aeolicus TilS, complexed with ATP, Mg(2+), and L-lysine, at 2.5 A resolution. The presence of the TilS-specific subdomain causes the active site to have two separate gateways, a large hole and a narrow tunnel on the opposite side. ATP is bound inside the hole, and L-lysine is bound at the entrance of the tunnel. The conserved Asp36 in the PP-motif coordinates Mg(2+). In these initial binding modes, the ATP, Mg(2+), and L-lysine are held far apart from each other, but they seem to be brought together for the reaction upon cytidine binding, with putative structural changes of the complex.

    Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Publishing Authors By Initials

    m kurataniM Kuratani,y yoshikawaY Yoshikawa,y besshoY Bessho,k higashijimaK Higashijima,t ishiiT Ishii,r shibataR Shibata,s takahashiS Takahashi,k yutaniK Yutani,s yokoyamaS Yokoyama,m kurataniM Kuratani,y yoshikawaY Yoshikawa,y besshoY Bessho,k higashijimaK Higashijima,t ishiiT Ishii,r shibataR Shibata,s takahashiS Takahashi,k yutaniK Yutani,s yokoyamaS Yokoyama,m kurataniM Kuratani,y yoshikawaY Yoshikawa,y besshoY Bessho,k higashijimaK Higashijima,t ishiiT Ishii,r shibataR Shibata,s takahashiS Takahashi,k yutaniK Yutani,s yokoyamaS Yokoyama,

    For similar abstracts research abstracts see: abstracts research

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    Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Structure (London, England : 1993)

    VOLUME: 15

    Page Numbers: 1642-53

    Journal Abbreviation: Structure

    ISSN: 0969-2126

    DAY: 12

    MONTH: Dec

    YEAR: 2007

    Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Information

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    LANGUAGE: eng

    NlmUniqueID: 101087697

    Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine. Keywords Mesh Terms:

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    Grant and Affiliation Information for Structural Basis of the Initial Binding of tRNA(Ile) Lysidine Synthetase TilS with ATP and L-Lysine.

    AFFILIATION: Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan; Genomic Sciences Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama, 230-0045, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Structure

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