6RV8

Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor covalent complex with the aldouronic acid UXXR

Summary for 6RV8

• Entry DOI: 10.2210/pdb6rv8/pdb
• Related: 6RTV 6RU1 6RU2 6RV7
• Related PRD ID: PRD_900116
• Descriptor: 4-O-methyl-glucuronoyl methylesterase, 4-O-methyl-alpha-D-glucopyranuronic acid-(1-2)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-Xylitol, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, ... (7 entities in total)
• Functional Keywords: ce15, esterase, alpha/beta-hydrolase, ligand-bound, hydrolase
• Biological source: Cerrena unicolor
• Total number of polymer chains: 2
• Total formula weight: 103998.96

Authors

Ernst, H.A.,Mosbech, C.,Langkilde, A.,Westh, P.,Meyer, A.,Agger, J.W.,Larsen, S. (deposition date: 2019-05-31, release date: 2020-03-18, Last modification date: 2024-11-13)

Primary citation

Ernst, H.A.,Mosbech, C.,Langkilde, A.E.,Westh, P.,Meyer, A.S.,Agger, J.W.,Larsen, S.
The structural basis of fungal glucuronoyl esterase activity on natural substrates.
Nat Commun, 11:1026-1026, 2020

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.

PubMed: 32094331
DOI: 10.1038/s41467-020-14833-9

Experimental method

X-RAY DIFFRACTION (1.85 Å)