Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK

Yasuhiro Arimura, Tomonori Kono, Kuniki Kino, Hitoshi Kurumizaka

    研究成果: Article

    抄録

    Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-α-l-glutamate peptides using l-glutamic acid. In the present study, the crystal structure of the Escherichia coli RimK protein complexed with the ATP analogue AMP-PNP was determined at 2.05 A - resolution. Two different conformations of RimK, closed and open forms, were observed in the crystals. The structural polymorphism revealed in this study provided important information to understand the mechanism by which RimK catalyzes the synthesis of poly-α- l-glutamate peptides and the polyglutamylation of ribosomal protein S6.

    元の言語English
    ページ(範囲)385-390
    ページ数6
    ジャーナルActa Crystallographica Section F: Structural Biology Communications
    74
    発行部数7
    DOI
    出版物ステータスPublished - 2018 7 1

    Fingerprint

    Glutamate Synthase (NADH)
    glutamates
    polymorphism
    Escherichia
    Polymorphism
    Ribosomal Protein S6
    Escherichia coli
    Glutamic Acid
    proteins
    peptides
    Adenylyl Imidodiphosphate
    adenosine monophosphate
    Peptides
    glutamic acid
    adenosine triphosphate
    Escherichia coli Proteins
    Protein Biosynthesis
    synthesis
    Conformations
    enzymes

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics

    これを引用

    Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK. / Arimura, Yasuhiro; Kono, Tomonori; Kino, Kuniki; Kurumizaka, Hitoshi.

    :: Acta Crystallographica Section F: Structural Biology Communications, 巻 74, 番号 7, 01.07.2018, p. 385-390.

    研究成果: Article

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    AU - Kurumizaka, Hitoshi

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