Structure of RizA, an l-amino-acid ligase from Bacillus subtilis

Wataru Kagawa, Toshinobu Arai, Shun Ishikura, Kuniki Kino, Hitoshi Kurumizaka

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    RizA is an l-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 Å resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies.

    Original languageEnglish
    Pages (from-to)1125-1130
    Number of pages6
    JournalActa Crystallographica Section F:Structural Biology Communications
    Volume71
    DOIs
    Publication statusPublished - 2015 Sep 1

    Fingerprint

    Bacillus
    Bacilli
    Ligases
    Bacillus subtilis
    amino acids
    Amino Acids
    Oligopeptides
    biosynthesis
    antibiotics
    Biosynthesis
    Binding Sites
    Anti-Bacterial Agents
    Substrates

    Keywords

    • ATP-grasp fold
    • dipeptide synthesis
    • l-amino-acid ligase
    • rhizocticin

    ASJC Scopus subject areas

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

    Cite this

    Structure of RizA, an l-amino-acid ligase from Bacillus subtilis. / Kagawa, Wataru; Arai, Toshinobu; Ishikura, Shun; Kino, Kuniki; Kurumizaka, Hitoshi.

    In: Acta Crystallographica Section F:Structural Biology Communications, Vol. 71, 01.09.2015, p. 1125-1130.

    Research output: Contribution to journalArticle

    Kagawa, Wataru ; Arai, Toshinobu ; Ishikura, Shun ; Kino, Kuniki ; Kurumizaka, Hitoshi. / Structure of RizA, an l-amino-acid ligase from Bacillus subtilis. In: Acta Crystallographica Section F:Structural Biology Communications. 2015 ; Vol. 71. pp. 1125-1130.
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    AU - Kurumizaka, Hitoshi

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