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Structural modeling of glucanase–substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-β-d-glucanases

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Abstract

Glycosyl hydrolase family 16 (GHF16) truncated Fibrobacter succinogenes (TFs) and GHF17 barley 1,3-1,4-β-d-glucanases (β-glucanases) possess different structural folds, β-jellyroll and (β/α)8, although they both catalyze the specific hydrolysis of β-1,4 glycosidic bonds adjacent to β-1,3 linkages in mixed β-1,3 and β-1,4 β-d-glucans or lichenan. Differences in the active site region residues of TFs β-glucanase and barley β-glucanase create binding site topographies that require different substrate conformations. In contrast to barley β-glucanase, TFs β-glucanase possesses a unique and compact active site. The structural analysis results suggest that the tyrosine residue, which is conserved in all known 1,3-1,4-β-d-glucanases, is involved in the recognition of mixed β-1,3 and β-1,4 linked polysaccharide.

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Acknowledgements

This work was supported by research grants from National Taipei University of Technology and National Science Council (NSC94-2311-B-027-001), Taipei, Taiwan, ROC.

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Authors and Affiliations

  1. Department of Molecular Science and Engineering, National Taipei University of Technology, Taipei, Taiwan

    Li-Chu Tsai

  2. Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan

    Yi-Ning Chen

  3. Agricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan

    Lie-Fen Shyur

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  1. Li-Chu Tsai
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  2. Yi-Ning Chen
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  3. Lie-Fen Shyur
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Correspondence to Li-Chu Tsai.

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Tsai, LC., Chen, YN. & Shyur, LF. Structural modeling of glucanase–substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-β-d-glucanases. J Comput Aided Mol Des 22, 915–923 (2008). https://doi.org/10.1007/s10822-008-9228-1

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