6KRL
Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris
Summary for 6KRL
| Entry DOI | 10.2210/pdb6krl/pdb |
| Descriptor | Mating factor alpha,GH30 Xylanase B, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | xylanase, glucuronoxylanase, hydrolase |
| Biological source | Saccharomyces uvarum (Yeast) More |
| Total number of polymer chains | 1 |
| Total formula weight | 62122.89 |
| Authors | Nakamichi, Y.,Watanabe, M.,Inoue, H. (deposition date: 2019-08-22, release date: 2020-06-17, Last modification date: 2024-10-09) |
| Primary citation | Nakamichi, Y.,Watanabe, M.,Matsushika, A.,Inoue, H. Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus. Febs Open Bio, 10:1180-1189, 2020 Cited by PubMed Abstract: Xylanase B, a member of subfamily 7 of the GH30 (glycoside hydrolase family 30) from Talaromyces cellulolyticus (TcXyn30B), is a bifunctional enzyme with glucuronoxylanase and xylobiohydrolase activities. In the present study, crystal structures of the native enzyme and the enzyme-product complex of TcXyn30B expressed in Pichia pastoris were determined at resolutions of 1.60 and 1.65 Å, respectively. The enzyme complexed with 2 -(4-O-methyl-α-d-glucuronyl)-xylobiose (U X) revealed that TcXyn30B strictly recognizes both the C-6 carboxyl group and the 4-O-methyl group of the 4-O-methyl-α-d-glucuronyl side chain by the conserved residues in GH30-7 endoxylanases. The crystal structure and site-directed mutagenesis indicated that Asn-93 on the β2-α2-loop interacts with the non-reducing end of the xylose residue at subsite-2 and is likely to be involved in xylobiohydrolase activity. These findings provide structural insight into the mechanisms of substrate recognition of GH30-7 glucuronoxylanase and xylobiohydrolase. PubMed: 32359208DOI: 10.1002/2211-5463.12873 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.601 Å) |
Structure validation
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