Abstract
α-l-Arabinofuranosidases, belonging to the glycoside hydrolase family (GH) 62, hydrolyze the α-1,2- or α-1,3-bond to liberate l-arabinofuranose from the xylan backbone. Here, we determined the structure of the C-terminal catalytic domain of CcAbf62A, a GH62 α-l-arabinofuranosidase from Coprinopsis cinerea. CcAbf62A is composed of a five-bladed β-propeller, as observed in other GH62 enzymes. The structure near the active site of CcAbf62A is also highly homologous to those of other GH62 enzymes. However, a calcium atom in the catalytic center interacts with an asparagine residue, Asn279, which is not found in other GH62 enzymes. In addition, some residues in subsites +3R, +2NR, +3NR, and +4NR of CcAbf62A are not conserved in other GH62 enzymes. In particular, a histidine residue, His221, is uniquely observed in subsite +2NR of CcAbf62A, which is likely to influence the substrate specificity. The results obtained here suggest that the amino acid residues that interact with the xylan backbone vary among the GH62 enzymes, despite the high similarity of their overall structures.
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Acknowledgments
This work was supported in part by a Grant-in-Aid for Scientific Research (no. 16K07687 to T.T. and no. 15H04526 to M.Y.) from the Japan Society for the Promotion of Science. This work has been performed under the approval of the Photon Factory Program Advisory Committee (Nos. 2014G512 and 2016G013).
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Tonozuka, T., Tanaka, Y., Okuyama, S. et al. Structure of the Catalytic Domain of α-l-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure–Function Relationships in Glycoside Hydrolase Family 62. Appl Biochem Biotechnol 181, 511–525 (2017). https://doi.org/10.1007/s12010-016-2227-0
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DOI: https://doi.org/10.1007/s12010-016-2227-0