The structural basis of fungal glucuronoyl esterase activity on natural substrates
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The structural basis of fungal glucuronoyl esterase activity on natural substrates. / Ernst, Heidi A; Mosbech, Caroline; Langkilde, Annette E; Westh, Peter; Meyer, Anne S; Wittrup Agger, Jane; Larsen, Sine.
I: Nature Communications, Bind 11, Nr. 1026, 2020, s. 1-12.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - The structural basis of fungal glucuronoyl esterase activity on natural substrates
AU - Ernst, Heidi A
AU - Mosbech, Caroline
AU - Langkilde, Annette E
AU - Westh, Peter
AU - Meyer, Anne S
AU - Wittrup Agger, Jane
AU - Larsen, Sine
PY - 2020
Y1 - 2020
N2 - 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.
AB - 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.
U2 - 10.1038/s41467-020-14833-9
DO - 10.1038/s41467-020-14833-9
M3 - Journal article
C2 - 32094331
VL - 11
SP - 1
EP - 12
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1026
ER -
ID: 236613895