Molecular modeling of family GH16 glycoside hydrolases: Potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae

Authors

  • Marco Strohmeier,

    1. Institute of Technical Biochemistry at the University of Stuttgart, D-70569 Stuttgart, Germany
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  • Maria Hrmova,

    1. Faculty of Sciences, School of Agriculture and Wine, and the Australian Centre for Plant Functional Genomics, The University of Adelaide, Glen Osmond, South Australia 5064, Australia
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  • Markus Fischer,

    1. Institute of Technical Biochemistry at the University of Stuttgart, D-70569 Stuttgart, Germany
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  • Andrew J. Harvey,

    1. Faculty of Sciences, School of Agriculture and Wine, and the Australian Centre for Plant Functional Genomics, The University of Adelaide, Glen Osmond, South Australia 5064, Australia
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  • Geoffrey B. Fincher,

    1. Faculty of Sciences, School of Agriculture and Wine, and the Australian Centre for Plant Functional Genomics, The University of Adelaide, Glen Osmond, South Australia 5064, Australia
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  • Jürgen Pleiss

    1. Institute of Technical Biochemistry at the University of Stuttgart, D-70569 Stuttgart, Germany
    2. Institute of Technical Biochemistry at the University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany; fax: +49-711-685-3195.
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Abstract

Family GH16 glycoside hydrolases can be assigned to five subgroups according to their substrate specificities, including xyloglucan transglucosylases/hydrolases (XTHs), (1,3)-β-galactanases, (1,4)-β-galactanases/κ-carrageenases, “nonspecific” (1,3/1,3;1,4)- β-d-glucan endohydrolases, and (1,3;1,4)-β-d-glucan endohydrolases. A structured family GH16 glycoside hydrolase database has been constructed (http://www.ghdb.uni-stuttgart.de) and provides multiple sequence alignments with functionally annotated amino acid residues and phylogenetic trees. The database has been used for homology modeling of seven glycoside hydrolases from the GH16 family with various substrate specificities, based on structural coordinates for (1,3;1,4)-β-d-glucan endohydrolases and a κ-carrageenase. In combination with multiple sequence alignments, the models predict the three-dimensional (3D) dispositions of amino acid residues in the substrate-binding and catalytic sites of XTHs and (1,3/1,3;1,4)-β-d-glucan endohydrolases; there is no structural information available in the databases for the latter group of enzymes. Models of the XTHs, compared with the recently determined structure of a Populus tremulos × tremuloides XTH, reveal similarities with the active sites of family GH11 (1,4)-β-d-xylan endohydrolases. From a biological viewpoint, the classification, molecular modeling and a new 3D structure of the P. tremulos × tremuloides XTH establish structural and evolutionary connections between XTHs, (1,3;1,4)-β-d-glucan endohydrolases and xylan endohydrolases. These findings raise the possibility that XTHs from higher plants could be active not only on cell wall xyloglucans, but also on (1,3;1,4)-β-d-glucans and arabinoxylans, which are major components of walls in grasses. A role for XTHs in (1,3;1,4)-β-d-glucan and arabinoxylan modification would be consistent with the apparent overrepresentation of XTH sequences in cereal expressed sequence tags databases.

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