High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
24 09 2020
24 09 2020
Historique:
received:
06
07
2020
accepted:
28
08
2020
entrez:
25
9
2020
pubmed:
26
9
2020
medline:
22
12
2020
Statut:
epublish
Résumé
Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products. Here we present the three-dimensional structure of a xylanase from Nectria haematococca (NhGH11) at 1.0 Å resolution and its functional properties. The atomic resolution structure provides details and insights about the complex hydrogen bonding network of the active site region and allowed a detailed comparison with homologous structures. Complementary biochemical studies showed that the xylanase can catalyze the hydrolysis of complex xylan into simple xylose aldopentose subunits of different lengths. NhGH11 can catalyze the efficient breakdown of beechwood xylan, xylan polysaccharide, and wheat arabinoxylan with turnover numbers of 1730.6 ± 318.1 min
Identifiants
pubmed: 32973265
doi: 10.1038/s41598-020-72644-w
pii: 10.1038/s41598-020-72644-w
pmc: PMC7519127
doi:
Substances chimiques
Metals
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
15658Références
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