6RU2
Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor
Summary for 6RU2
| Entry DOI | 10.2210/pdb6ru2/pdb |
| Related | 6RTV 6RU1 |
| Descriptor | 4-O-methyl-glucuronoyl methylesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (7 entities in total) |
| Functional Keywords | ce15, esterase, alpha/beta-hydrolase, hydrolase |
| Biological source | Cerrena unicolor |
| Total number of polymer chains | 2 |
| Total formula weight | 88056.50 |
| Authors | Ernst, H.A.,Mosbech, C.,Langkilde, A.,Westh, P.,Meyer, A.,Agger, J.W.,Larsen, S. (deposition date: 2019-05-27, release date: 2020-03-18, Last modification date: 2024-10-09) |
| 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 Cited by 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: 32094331DOI: 10.1038/s41467-020-14833-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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