8J9F
Structure of STG-hydrolyzing beta-glucosidase 1 (PSTG1)
Summary for 8J9F
| Entry DOI | 10.2210/pdb8j9f/pdb |
| Descriptor | Beta-glucosidase, GLYCEROL (3 entities in total) |
| Functional Keywords | gh3 family, sesaminol biosynthesis, hydrolase |
| Biological source | Paenibacillus relictisesami (Paenibacillus sp. KB0549) |
| Total number of polymer chains | 4 |
| Total formula weight | 346798.03 |
| Authors | Yanai, T.,Imaizumi, R.,Takahashi, Y.,Katsumura, E.,Yamamoto, M.,Nakayama, T.,Yamashita, S.,Takeshita, K.,Sakai, N.,Matsuura, H. (deposition date: 2023-05-03, release date: 2024-04-10, Last modification date: 2024-07-17) |
| Primary citation | Yanai, T.,Takahashi, Y.,Katsumura, E.,Sakai, N.,Takeshita, K.,Imaizumi, R.,Matsuura, H.,Hongo, S.,Waki, T.,Takahashi, S.,Yamamoto, M.,Kataoka, K.,Nakayama, T.,Yamashita, S. Structural insights into a bacterial beta-glucosidase capable of degrading sesaminol triglucoside to produce sesaminol: toward the understanding of the aglycone recognition mechanism by the C-terminal lid domain. J.Biochem., 174:335-344, 2023 Cited by PubMed Abstract: The sesaminol triglucoside (STG)-hydrolyzing β-glucosidase from Paenibacillus sp. (PSTG1), which belongs to glycoside hydrolase family 3 (GH3), is a promising catalyst for the industrial production of sesaminol. We determined the X-ray crystal structure of PSTG1 with bound glycerol molecule in the putative active site. PSTG1 monomer contained typical three domains of GH3 with the active site in domain 1 (TIM barrel). In addition, PSTG1 contained an additional domain (domain 4) at the C-terminus that interacts with the active site of the other protomer as a lid in the dimer unit. Interestingly, the interface of domain 4 and the active site forms a hydrophobic cavity probably for recognizing the hydrophobic aglycone moiety of substrate. The short flexible loop region of TIM barrel was found to be approaching the interface of domain 4 and the active site. We found that n-heptyl-β-D-thioglucopyranoside detergent acts as an inhibitor for PSTG1. Thus, we propose that the recognition of hydrophobic aglycone moiety is important for PSTG1-catalyzed reactions. Domain 4 might be a potential target for elucidating the aglycone recognition mechanism of PSTG1 as well as for engineering PSTG1 to create a further excellent enzyme to degrade STG more efficiently to produce sesaminol. PubMed: 37384427DOI: 10.1093/jb/mvad048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
Download full validation report
