5YJ7
Structural insight into the beta-GH1 glucosidase BGLN1 from oleaginous microalgae Nannochloropsis
Summary for 5YJ7
| Entry DOI | 10.2210/pdb5yj7/pdb |
| Descriptor | Glycoside hydrolase, CALCIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | glycoside hydrolase, beta-1, 3-glucan, substrate specificity, carbohydrate, hydrolase |
| Biological source | Nannochloris |
| Total number of polymer chains | 4 |
| Total formula weight | 233834.10 |
| Authors | Dong, S.,Liu, Y.J.,Zhou, H.X.,Xiao, Y.,Xu, J.,Cui, Q.,Wang, X.Q.,Feng, Y.G. (deposition date: 2017-10-09, release date: 2018-10-10, Last modification date: 2024-10-09) |
| Primary citation | Dong, S.,Liu, Y.J.,Zhou, H.,Xiao, Y.,Xu, J.,Cui, Q.,Wang, X.,Feng, Y. Structural insight into a GH1 beta-glucosidase from the oleaginous microalga, Nannochloropsis oceanica. Int.J.Biol.Macromol., 170:196-206, 2021 Cited by PubMed Abstract: Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved -1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. PubMed: 33347927DOI: 10.1016/j.ijbiomac.2020.12.128 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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