title: Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form.
abstract: 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 2.8 Å 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.
authors.affiliation: Biomass Refinery Research Center, National Institute of Advanced Industrial Science, 3-11-32 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-0046, Japan.
authors.forename: Makoto
authors.initials: M
authors.lastname: Nakabayashi
authors.affiliation: Biomass Refinery Research Center, National Institute of Advanced Industrial Science, 3-11-32 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-0046, Japan.
authors.forename: Misumi
authors.initials: M
authors.lastname: Kataoka
authors.affiliation: Biomass Refinery Research Center, National Institute of Advanced Industrial Science, 3-11-32 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-0046, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Watanabe
authors.affiliation: Biomass Refinery Research Center, National Institute of Advanced Industrial Science, 3-11-32 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-0046, Japan.
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ishikawa
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006358:Hot Temperature; D008958:Models, Molecular; D008970:Molecular Weight; D009154:Mutation; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020027:Pyrococcus furiosus / Q000737:chemistry* / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001617:beta-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D001617:beta-Glucosidase
keywords: Pyrococcus furiosus; intersubunit interactions; thermostable enzyme; β-glucosidases