The structural basis of fungal glucuronoyl esterase activity on natural substrates

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Nature Communications, Vol. 11, No. 1026, 2020, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Ernst, HA, Mosbech, C, Langkilde, AE, Westh, P, Meyer, AS, Wittrup Agger, J & Larsen, S 2020, 'The structural basis of fungal glucuronoyl esterase activity on natural substrates', Nature Communications, vol. 11, no. 1026, pp. 1-12. https://doi.org/10.1038/s41467-020-14833-9

APA

Ernst, H. A., Mosbech, C., Langkilde, A. E., Westh, P., Meyer, A. S., Wittrup Agger, J., & Larsen, S. (2020). The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nature Communications, 11(1026), 1-12. https://doi.org/10.1038/s41467-020-14833-9

Vancouver

Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Wittrup Agger J et al. The structural basis of fungal glucuronoyl esterase activity on natural substrates. Nature Communications. 2020;11(1026):1-12. https://doi.org/10.1038/s41467-020-14833-9

Author

Ernst, Heidi A ; Mosbech, Caroline ; Langkilde, Annette E ; Westh, Peter ; Meyer, Anne S ; Wittrup Agger, Jane ; Larsen, Sine. / The structural basis of fungal glucuronoyl esterase activity on natural substrates. In: Nature Communications. 2020 ; Vol. 11, No. 1026. pp. 1-12.

Bibtex

@article{c937a71538654065b5cee67debb651f0,
title = "The structural basis of fungal glucuronoyl esterase activity on natural substrates",
abstract = "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.",
author = "Ernst, {Heidi A} and Caroline Mosbech and Langkilde, {Annette E} and Peter Westh and Meyer, {Anne S} and {Wittrup Agger}, Jane and Sine Larsen",
year = "2020",
doi = "10.1038/s41467-020-14833-9",
language = "English",
volume = "11",
pages = "1--12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1026",

}

RIS

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