8X3U
tll1591 with alpha_glucan 3sugar
Summary for 8X3U
| Entry DOI | 10.2210/pdb8x3u/pdb |
| Descriptor | Glycosyl transferase, alpha-D-glucopyranose-(1-2)-alpha-D-glucopyranose-(1-2)-beta-D-fructofuranose, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | tll1591 with alpha_glucan 3sugar, transferase |
| Biological source | Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) |
| Total number of polymer chains | 4 |
| Total formula weight | 165266.12 |
| Authors | Su, J.Y. (deposition date: 2023-11-14, release date: 2024-10-16, Last modification date: 2025-04-30) |
| Primary citation | Qu, X.,An, Q.,Sayed, H.,Cui, L.,Mayo, K.H.,Su, J.Y. Glucosyltransferase TeGSS from Thermosynechococcus elongatus produces an alpha-1,2-glucan. Int.J.Biol.Macromol., 280:136152-136152, 2024 Cited by PubMed Abstract: Here, we enzymatically produced a novel α-1,2-glucan, glucosylsucrose, that has a chemical structure significantly different from that of other glucans. This structural difference suggests its potential to modulate new physiological activities compared to known glucans. The enzyme TeGSS catalyzes the synthesis of this α-1,2-glucan from sucrose and UDP-glucose (UDPG). Using NMR spectroscopy, we elucidated the chemical structures of TeGSS-synthesized glucosylsucrose tri-, tetra-, and penta-saccharides in which the monosaccharide units are linked by α-1,2-glycosidic bonds. We also report the crystal structures of TeGSS co-crystallized with UDP and glucosylsucrose tri- and tetra-saccharides. Site-directed mutagenesis of residues in and around the TeGSS catalytic center has allowed us to propose a concerted Si mechanism of action. Finally, we developed an enzyme-coupled reaction involving TeGSS and SuSyAc that allows production of UDPG for the synthesis of α-1,2-glucan. PubMed: 39357710DOI: 10.1016/j.ijbiomac.2024.136152 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.58 Å) |
Structure validation
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