6GU8
Glucuronoyl Esterase from Solibacter usitatus
Summary for 6GU8
| Entry DOI | 10.2210/pdb6gu8/pdb |
| Descriptor | Putative acetyl xylan esterase, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | carbohydrate esterase, hydrolase |
| Biological source | Candidatus Solibacter usitatus Ellin6076 |
| Total number of polymer chains | 1 |
| Total formula weight | 45028.51 |
| Authors | Lo Leggio, L.,Larsbrink, J.,Meland Knudsen, R.,Mazurkewich, S.,Navarro Poulsen, J.C. (deposition date: 2018-06-19, release date: 2018-08-15, Last modification date: 2024-10-16) |
| Primary citation | Arnling Baath, J.,Mazurkewich, S.,Knudsen, R.M.,Poulsen, J.N.,Olsson, L.,Lo Leggio, L.,Larsbrink, J. Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion. Biotechnol Biofuels, 11:213-213, 2018 Cited by PubMed Abstract: Lignocellulose is highly recalcitrant to enzymatic deconstruction, where the recalcitrance primarily results from chemical linkages between lignin and carbohydrates. Glucuronoyl esterases (GEs) from carbohydrate esterase family 15 (CE15) have been suggested to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan. However, only a limited number of GEs have been biochemically characterized and structurally determined to date, limiting our understanding of these enzymes and their potential exploration. PubMed: 30083226DOI: 10.1186/s13068-018-1213-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01807823457 Å) |
Structure validation
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