8IDP
Crystal structure of reducing-end xylose-releasing exoxylanase in GH30 from Talaromyces cellulolyticus
Summary for 8IDP
| Entry DOI | 10.2210/pdb8idp/pdb |
| Descriptor | Reducing-end xylose-releasing exoxylanase Xyn30A, TETRAETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (12 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Talaromyces pinophilus |
| Total number of polymer chains | 4 |
| Total formula weight | 220476.12 |
| Authors | Nakamichi, Y.,Watanabe, M.,Fujii, T.,Inoue, H.,Morita, T. (deposition date: 2023-02-14, release date: 2023-05-17, Last modification date: 2024-11-20) |
| Primary citation | Nakamichi, Y.,Watanabe, M.,Fujii, T.,Inoue, H.,Morita, T. Crystal structure of reducing-end xylose-releasing exoxylanase in subfamily 7 of glycoside hydrolase family 30. Proteins, 91:1341-1350, 2023 Cited by PubMed Abstract: TcXyn30A from Talaromyces cellulolyticus, which belongs to subfamily 7 of the glycoside hydrolase family 30 (GH30-7), releases xylose from the reducing end of xylan and xylooligosaccharides (XOSs), the so-called reducing-end xylose-releasing exoxylanase (ReX). In this study, the crystal structures of TcXyn30A with and without xylose at subsite +1 (the binding site of the xylose residue at the reducing end) were determined. This is the first report on the structure of ReX in the family GH30-7. TcXyn30A forms a dimer. The complex structure of TcXyn30A with xylose revealed that subsite +1 is located at the dimer interface. TcXyn30A recognizes xylose at subsite +1 composed of amino acid residues from each monomer and blocks substrate binding to subsite +2 by dimer formation. Thus, the dimeric conformation is responsible for ReX activity. The structural comparison between TcXyn30A and the homologous enzyme indicated that subsite -2 is composed of assembled three stacked Trp residues, Trp49, Trp333, and Trp334, allowing TcXyn30A to accommodate xylan and any branched XOSs decorated with a substitution such as α-1,2-linked 4-O-methyl-d-glucuronic acid or α-1,2- and/or -1,3-linked L-arabinofuranose. These findings provide an insight into the structural determinants for ReX activity of TcXyn30A. PubMed: 37144255DOI: 10.1002/prot.26505 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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