Crystal Structures of Glycoside Hydrolase Family 51 α-<small>L</small>-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

doi:10.1271/bbb.110902

This article has now been updated. Please use the final version.

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

Author information

Do-Hyun IM
Department of Biotechnology, The University of Tokyo
Kei-ichi KIMURA
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Fumitaka HAYASAKA
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Tomonari TANAKA
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Masato NOGUCHI
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Atsushi KOBAYASHI
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Shin-ichiro SHODA
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University
Kentaro MIYAZAKI
Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST)
Takayoshi WAKAGI
Department of Biotechnology, The University of Tokyo
Shinya FUSHINOBU
Department of Biotechnology, The University of Tokyo

Keywords: α-L-arabinofuranosidase, Thermotoga maritima, glycoside hydrolase family 51, arabinose, xylose

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Supplementary material

Article ID: 110902

DOI https://doi.org/10.1271/bbb.110902

The final version of this article is now available: Vol. 76 (2012) , No. 2 p.423

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Abstract

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 1.8–2.3 Å resolution to determine the architecture of the substrate binding pocket. Subsite −1 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.

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