Download MendeleyThe structural basis of fungal glucuronoyl esterase activity on natural substrates.
Ernst, H.A., Mosbech, C., Langkilde, A.E., Westh, P., Meyer, A.S., Agger, J.W., Larsen, S.(2020) Nat Commun 11: 1026-1026
- PubMed: 32094331
- DOI: https://doi.org/10.1038/s41467-020-14833-9
- Primary Citation of Related Structures:
6RTV, 6RU1, 6RU2, 6RV7, 6RV8, 6RV9 - PubMed 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.
Organizational Affiliation:
Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen Ø, Denmark.
