Substrate binding to a GH131 β-glucanase catalytic domain from Podospora anserina |
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Authors: | Tong Jiang Hsiu-Chien Chan Chun-Hsiang Huang Tzu-Ping Ko Ting-Yung Huang Je-Ruei Liu Rey-Ting Guo |
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Institution: | 1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China;2. Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan;3. Genozyme biotechnology Inc., Taipei 106, Taiwan;4. AsiaPac Biotechnology Co., Ltd., Dongguan 523808, China;5. Institute of Biotechnology, National Taiwan University, Taipei 106, Taiwan |
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Abstract: | β-Glucanases have been utilized widely in industry to treat various carbohydrate-containing materials. Recently, the Podospora anserina β-glucanase 131A (PaGluc131A) was identified and classified to a new glycoside hydrolases GH131 family. It shows exo-β-1,3/exo-β-1,6 and endo-β-1,4 glucanase activities with a broad substrate specificity for laminarin, curdlan, pachyman, lichenan, pustulan, and cellulosic derivatives. Here we report the crystal structures of the PaGluc131A catalytic domain with or without ligand (cellotriose) at 1.8 Å resolution. The cellotriose was clearly observed to occupy the +1 to +3 subsites in substrate binding cleft. The broadened substrate binding groove may explain the diverse substrate specificity. Based on our crystal structures, the GH131 family enzyme is likely to carry out the hydrolysis through an inverting catalytic mechanism, in which E99 and E139 are supposed to serve as the general base and general acid. |
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Keywords: | Glycoside hydrolase Crystal structure β-Glucanase GH131 |
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