The structural basis of fungal glucuronoyl esterase activity on natural substrates.
Carbohydrates
Catalytic Domain
Cell Wall
/ metabolism
Crystallography, X-Ray
Esterases
/ isolation & purification
Fungal Proteins
/ isolation & purification
Glucuronic Acid
/ metabolism
Hydrolysis
Lignin
/ metabolism
Polyporales
/ enzymology
Protein Structure, Secondary
Recombinant Proteins
/ isolation & purification
Scattering, Small Angle
Structure-Activity Relationship
Substrate Specificity
X-Ray Diffraction
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
24 02 2020
24 02 2020
Historique:
received:
16
09
2019
accepted:
06
02
2020
entrez:
26
2
2020
pubmed:
26
2
2020
medline:
6
5
2020
Statut:
epublish
Résumé
Structural and functional studies were conducted of the glucuronoyl esterase (GE) from Cerrena unicolor (CuGE), an enzyme catalyzing cleavage of lignin-carbohydrate ester bonds. CuGE is an α/β-hydrolase belonging to carbohydrate esterase family 15 (CE15). The enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. SAXS data show CuGE as an elongated rigid molecule where the two domains are connected by a rigid linker. Detailed structural information of the catalytic domain in its apo- and inactivated form and complexes with aldouronic acids reveal well-defined binding of the 4-O-methyl-a-D-glucuronoyl moiety, not influenced by the nature of the attached xylo-oligosaccharide. Structural and sequence comparisons within CE15 enzymes reveal two distinct structural subgroups. CuGE belongs to the group of fungal CE15-B enzymes with an open and flat substrate-binding site. The interactions between CuGE and its natural substrates are explained and rationalized by the structural results, microscale thermophoresis and isothermal calorimetry.
Identifiants
pubmed: 32094331
doi: 10.1038/s41467-020-14833-9
pii: 10.1038/s41467-020-14833-9
pmc: PMC7039992
doi:
Substances chimiques
Carbohydrates
0
Fungal Proteins
0
Recombinant Proteins
0
lignocellulose
11132-73-3
Glucuronic Acid
8A5D83Q4RW
Lignin
9005-53-2
Esterases
EC 3.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1026Références
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