7VEL
Crystal structure of Phytolacca americana UGT3 with UDP-2fluoroglucose
Summary for 7VEL
| Entry DOI | 10.2210/pdb7vel/pdb |
| Descriptor | Glycosyltransferase, 1,2-ETHANEDIOL, 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE, ... (6 entities in total) |
| Functional Keywords | ugt, glycosyltransferase, udp-2fglc, transferase |
| Biological source | Phytolacca americana (American pokeweed) |
| Total number of polymer chains | 2 |
| Total formula weight | 116761.65 |
| Authors | Maharjan, R.,Fukuda, Y.,Nakayama, T.,Nakayama, T.,Hamada, H.,Ozaki, S.,Inoue, T. (deposition date: 2021-09-09, release date: 2022-03-02, Last modification date: 2023-11-29) |
| Primary citation | Maharjan, R.,Fukuda, Y.,Nakayama, T.,Nakayama, T.,Hamada, H.,Ozaki, S.I.,Inoue, T. Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3. Acta Crystallogr D Struct Biol, 78:379-389, 2022 Cited by PubMed Abstract: Capsaicinoids are phenolic compounds that have health benefits. However, the pungency and poor water solubility of these compounds limit their exploitation. Glycosylation is a powerful method to improve water solubility and reduce pungency while preserving bioactivity. PaGT3, a uridine diphosphate glycosyltransferase (UGT) from Phytolacca americana, is known for its ability to glycosylate capsaicinoids and other phenolic compounds. While structural information on several UGTs is available, structures of UGTs that can glycosylate a range of phenolic compounds are rare. To fill this gap, crystal structures of PaGT3 with a sugar-donor analogue (UDP-2-fluoroglucose) and the acceptors capsaicin and kaempferol were determined. PaGT3 adopts a GT-B-fold structure that is highly conserved among UGTs. However, the acceptor-binding pocket in PaGT3 is hydrophobic and large, and is surrounded by longer loops. The larger acceptor-binding pocket in PaGT3 allows the enzyme to bind a range of compounds, while the flexibility of the longer loops possibly plays a role in accommodating the acceptors in the binding pocket according to their shape and size. This structural information provides insights into the acceptor-binding mechanism in UGTs that bind multiple substrates. PubMed: 35234151DOI: 10.1107/S2059798322000869 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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