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6KRN

Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid

Summary for 6KRN
Entry DOI10.2210/pdb6krn/pdb
Related6KRL
DescriptorMating factor alpha,GH30 Xylanase B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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, ... (6 entities in total)
Functional Keywordsxylanase, glucuronoxylanase, hydrolase
Biological sourceSaccharomyces uvarum (Yeast)
More
Total number of polymer chains1
Total formula weight63030.66
Authors
Nakamichi, Y.,Watanabe, M.,Inoue, H. (deposition date: 2019-08-22, release date: 2020-06-17, Last modification date: 2023-11-22)
Primary citationNakamichi, 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: 32359208
DOI: 10.1002/2211-5463.12873
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.653 Å)
Structure validation

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数据于2024-10-30公开中

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