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

ABSTRACT: One of the ?-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.

SUBMITTER: Nakabayashi M

PROVIDER: S-EPMC4089520 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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

Nakabayashi Makoto M Kataoka Misumi M Watanabe Masahiro M Ishikawa Kazuhiko K

Acta crystallographica. Section F, Structural biology communications 20140618 Pt 7

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 consist ...[more]

PMID: 25005077

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