Summary for 4HZ8
| Entry DOI | 10.2210/pdb4hz8/pdb |
| Related | 4HZ6 4HZ7 |
| Descriptor | Beta-glucosidase, beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | glucosidase, beta-glucosidase, bglb, bgl, hydrolase, glycosidase, tim barrel, carbohydrate/sugar binding |
| Biological source | Uncultured bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 50474.43 |
| Authors | Hwang, K.Y.,Nam, K.H. (deposition date: 2012-11-14, release date: 2012-12-19, Last modification date: 2023-11-08) |
| Primary citation | Nam, K.H.,Sung, M.W.,Hwang, K.Y. Structural insights into the substrate recognition properties of beta-glucosidase. Biochem.Biophys.Res.Commun., 391:1131-1135, 2010 Cited by PubMed Abstract: Beta-glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that beta-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of beta-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of beta-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of beta-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of beta-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of beta-glucosidase. PubMed: 20005197DOI: 10.1016/j.bbrc.2009.12.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.14 Å) |
Structure validation
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