Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium.
GH11 xylobiohydrolase
atypical substrate recognition
lignocellulosic biomass
metatranscriptome
plant cell wall degrading enzymes
x-ray crystallography
Journal
Biotechnology and bioengineering
ISSN: 1097-0290
Titre abrégé: Biotechnol Bioeng
Pays: United States
ID NLM: 7502021
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
revised:
28
06
2021
received:
25
02
2021
accepted:
04
07
2021
pubmed:
8
7
2021
medline:
3
3
2022
entrez:
7
7
2021
Statut:
ppublish
Résumé
The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-β-1,4-xylanases, β-xylosidases, acetylxylan esterases, α-l-arabinofuranosidases, and α-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-β-1,4- and β-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase.
Substances chimiques
Disaccharides
0
Xylans
0
lignocellulose
11132-73-3
Lignin
9005-53-2
Glycoside Hydrolases
EC 3.2.1.-
xylobiose
ID02R0EG7P
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4052-4064Informations de copyright
© 2021 Wiley Periodicals LLC.
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