9GCI
The crystal structure of beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus determined at 1.47 A resolution
Summary for 9GCI
| Entry DOI | 10.2210/pdb9gci/pdb |
| Descriptor | beta-glucosidase, GLYCEROL, 1,2-ETHANEDIOL, ... (8 entities in total) |
| Functional Keywords | biocatalysis, beta-glucosidase, caldicellulosiruptor saccharolyticus, hydrolase |
| Biological source | Caldicellulosiruptor saccharolyticus DSM 8903 |
| Total number of polymer chains | 2 |
| Total formula weight | 109991.97 |
| Authors | |
| Primary citation | Sotiropoulou, A.I.,Hatzinikolaou, D.G.,Chrysina, E.D. Structural studies of beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus. Acta Crystallogr D Struct Biol, 80:733-743, 2024 Cited by PubMed Abstract: β-Glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus (Bgl1) has been denoted as having an attractive catalytic profile for various industrial applications. Bgl1 catalyses the final step of in the decomposition of cellulose, an unbranched glucose polymer that has attracted the attention of researchers in recent years as it is the most abundant renewable source of reduced carbon in the biosphere. With the aim of enhancing the thermostability of Bgl1 for a broad spectrum of biotechnological processes, it has been subjected to structural studies. Crystal structures of Bgl1 and its complex with glucose were determined at 1.47 and 1.95 Å resolution, respectively. Bgl1 is a member of glycosyl hydrolase family 1 (GH1 superfamily, EC 3.2.1.21) and the results showed that the 3D structure of Bgl1 follows the overall architecture of the GH1 family, with a classical (β/α) TIM-barrel fold. Comparisons of Bgl1 with sequence or structural homologues of β-glucosidase reveal quite similar structures but also unique structural features in Bgl1 with plausible functional roles. PubMed: 39361356DOI: 10.1107/S2059798324009252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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