4G4G
Crystal structure of recombinant glucuronoyl esterase from Sporotrichum thermophile determined at 1.55 A resolution
Summary for 4G4G
| Entry DOI | 10.2210/pdb4g4g/pdb |
| Related | 4G4I 4G4J |
| Descriptor | 4-O-methyl-glucuronoyl methylesterase, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | alpha/beta hydrolase, 3-layer alpha/beta/alpha sandwich, rossmann fold, glucuronoyl esterase, hydrolase |
| Biological source | Myceliophthora thermophila |
| Cellular location | Secreted (Probable): G2QJR6 |
| Total number of polymer chains | 1 |
| Total formula weight | 47115.31 |
| Authors | Charavgi, M.D.,Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D. (deposition date: 2012-07-16, release date: 2013-01-02, Last modification date: 2024-11-06) |
| Primary citation | Charavgi, M.D.,Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D. The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst. Acta Crystallogr.,Sect.D, 69:63-73, 2013 Cited by PubMed Abstract: The increasing demand for the development of efficient biocatalysts is a consequence of their broad industrial applications. Typical difficulties that are encountered during their exploitation in a variety of processes are interconnected with factors such as temperature, pH, product inhibitors etc. To eliminate these, research has been directed towards the identification of new enzymes that would comply with the required standards. To this end, the recently discovered glucuronoyl esterases (GEs) are an enigmatic family within the carbohydrate esterase (CE) family. Structures of the thermophilic StGE2 esterase from Myceliophthora thermophila (synonym Sporotrichum thermophile), a member of the CE15 family, and its S213A mutant were determined at 1.55 and 1.9 Å resolution, respectively. The first crystal structure of the S213A mutant in complex with a substrate analogue, methyl 4-O-methyl-β-D-glucopyranuronate, was determined at 2.35 Å resolution. All of the three-dimensional protein structures have an α/β-hydrolase fold with a three-layer αβα-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. These are the first crystal structures of a thermophilic GE both in an unliganded form and bound to a substrate analogue, thus unravelling the organization of the catalytic triad residues and their neighbours lining the active site. The knowledge derived offers novel insights into the key structural elements that drive the hydrolysis of glucuronic acid esters. PubMed: 23275164DOI: 10.1107/S0907444912042400 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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