Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form

Makoto Nakabayashi, Misumi Kataoka, Masahiro Watanabe, Kazuhiko Ishikawa

Research output: Contribution to journalArticle


One of the β-glucosidases from Pyrococcus furiosus (BGLPf) is found to be a hyperthermophilic tetrameric enzyme that can degrade cellooligosaccharides. Recently, the crystal structures of the tetrameric and dimeric forms were solved. Here, a new monomeric form of BGLPf was constructed by removing the C-terminal region of the enzyme and its crystal structure was solved at a resolution of 2.8Å in space group P1. It was discovered that the mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. Under biological conditions, the mutant enzyme forms a monomer. This result helps explain how BGLPf has attained its oligomeric structure and thermostability.

Original languageEnglish
Pages (from-to)854-859
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number7
Publication statusPublished - Jul 2014



  • Pyrococcus furiosus
  • intersubunit interactions
  • thermostable enzyme
  • β-glucosidases

ASJC Scopus subject areas

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

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