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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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
Publication statusPublished - 2015 Sept 1


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

ASJC Scopus subject areas

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


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