Crystal structures of glycoside hydrolase family 51 α-L- arabinofuranosidase from Thermotoga maritima

Do Hyun Im, Kei Ichi Kimura, Fumitaka Hayasaka, Tomonari Tanaka, Masato Noguchi, Atsushi Kobayashi, Shin Ichiro Shoda, Kentaro Miyazaki, Takayoshi Wakagi, Shinya Fushinobu

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


α-L-Arabinofuranosidase from the hyperthermophilic bacterium Thermotoga maritima (Tm-AFase) is an extremely thermophilic enzyme belonging to glycoside hydrolase family 51. It can catalyze the transglycosylation of a novel glycosyl donor, 4,6-dimethoxy-1,3,5-triazin-2-yl (DMT)-β-D-xylopyranoside. In this study we determined the crystal structures of Tm-AFase in substrate-free and complex forms with arabinose and xylose at 1.8-2.3Å resolution to determine the architecture of the substrate binding pocket. Subsite α1 of Tm-AFase is similar to that of α-L-arabinofuranosidase from Geobacillus stearothermophilus, but the substrate binding pocket of Tm-AFase is narrower and more hydrophobic. Possible substrate binding modes were investigated by automated docking analysis.

Original languageEnglish
Pages (from-to)423-428
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Issue number2
Publication statusPublished - 2012
Externally publishedYes


  • Arabinose
  • Glycoside hydrolase family 51
  • Thermotoga maritima
  • Xylose
  • α-L-arabinofuranosidase

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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