Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus.
Amino Acid Sequence
/ genetics
Crystallography, X-Ray
Endo-1,4-beta Xylanases
/ genetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation, alpha-Helical
/ genetics
Protein Conformation, beta-Strand
/ genetics
Recombinant Proteins
/ genetics
Saccharomycetales
Sequence Alignment
Substrate Specificity
Talaromyces
/ enzymology
Xylans
/ metabolism
Talaromyces cellulolyticus
crystal structure
enzyme-product complex
glucuronoxylanase
glycoside hydrolase family 30
xylobiohydrolase
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
03
03
2020
revised:
23
04
2020
accepted:
28
04
2020
pubmed:
3
5
2020
medline:
20
7
2021
entrez:
3
5
2020
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 32359208
doi: 10.1002/2211-5463.12873
pmc: PMC7262913
doi:
Substances chimiques
Recombinant Proteins
0
Xylans
0
Endo-1,4-beta Xylanases
EC 3.2.1.8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1180-1189Informations de copyright
© 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
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