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

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 2.8Å 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
Volume70
Issue number7
DOIs
Publication statusPublished - 2014
Externally publishedYes

Fingerprint

Glucosidases
enzymes
monomers
Monomers
Crystals
Enzymes
crystals
Crystal structure
Pyrococcus furiosus
crystal structure
thermal stability
rings

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology
  • Condensed Matter Physics
  • Medicine(all)

Cite this

Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form. / Nakabayashi, Makoto; Kataoka, Misumi; Watanabe, Masahiro; Ishikawa, Kazuhiko.

In: Acta Crystallographica Section F:Structural Biology Communications, Vol. 70, No. 7, 2014, p. 854-859.

Research output: Contribution to journalArticle

Nakabayashi, Makoto ; Kataoka, Misumi ; Watanabe, Masahiro ; Ishikawa, Kazuhiko. / Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form. In: Acta Crystallographica Section F:Structural Biology Communications. 2014 ; Vol. 70, No. 7. pp. 854-859.
@article{71964205700544b7af2cd31f49268b9e,
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{\AA} 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.",
keywords = "intersubunit interactions, Pyrococcus furiosus, thermostable enzyme, β-glucosidases",
author = "Makoto Nakabayashi and Misumi Kataoka and Masahiro Watanabe and Kazuhiko Ishikawa",
year = "2014",
doi = "10.1107/S2053230X14010188",
language = "English",
volume = "70",
pages = "854--859",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "7",

}

TY - JOUR

T1 - Monomer structure of a hyperthermophilic β-glucosidase mutant forming a dodecameric structure in the crystal form

AU - Nakabayashi, Makoto

AU - Kataoka, Misumi

AU - Watanabe, Masahiro

AU - Ishikawa, Kazuhiko

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

KW - intersubunit interactions

KW - Pyrococcus furiosus

KW - thermostable enzyme

KW - β-glucosidases

UR - http://www.scopus.com/inward/record.url?scp=84905474530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84905474530&partnerID=8YFLogxK

U2 - 10.1107/S2053230X14010188

DO - 10.1107/S2053230X14010188

M3 - Article

C2 - 25005077

AN - SCOPUS:84905474530

VL - 70

SP - 854

EP - 859

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 7

ER -