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

研究成果: Article査読

13 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)423-428
ページ数6
ジャーナルBioscience, Biotechnology and Biochemistry
76
2
DOI
出版ステータスPublished - 2012

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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