6L5R
crystal structure of GgCGT in complex with UDP-Glu
Summary for 6L5R
| Entry DOI | 10.2210/pdb6l5r/pdb |
| Descriptor | GgCGT, URIDINE-5'-DIPHOSPHATE, 3-(4-HYDROXYPHENYL)-1-(2,4,6-TRIHYDROXYPHENYL)PROPAN-1-ONE (3 entities in total) |
| Functional Keywords | di-c-glycosyltransferase, transferase |
| Biological source | Glycyrrhiza glabra |
| Total number of polymer chains | 1 |
| Total formula weight | 52771.50 |
| Authors | |
| Primary citation | Zhang, M.,Li, F.D.,Li, K.,Wang, Z.L.,Wang, Y.X.,He, J.B.,Su, H.F.,Zhang, Z.Y.,Chi, C.B.,Shi, X.M.,Yun, C.H.,Zhang, Z.Y.,Liu, Z.M.,Zhang, L.R.,Yang, D.H.,Ma, M.,Qiao, X.,Ye, M. Functional Characterization and Structural Basis of an Efficient Di-C-glycosyltransferase fromGlycyrrhiza glabra. J.Am.Chem.Soc., 142:3506-3512, 2020 Cited by PubMed Abstract: A highly efficient di--glycosyltransferase GgCGT was discovered from the medicinal plant . GgCGT catalyzes a two-step di--glycosylation of flopropione-containing substrates with conversion rates of >98%. To elucidate the catalytic mechanisms of GgCGT, we solved its crystal structures in complex with UDP-Glc, UDP-Gal, UDP/phloretin, and UDP/nothofagin, respectively. Structural analysis revealed that the sugar donor selectivity was controlled by the hydrogen-bond interactions of sugar hydroxyl groups with D390 and other key residues. The di--glycosylation capability of GgCGT was attributed to a spacious substrate-binding tunnel, and the G389K mutation could switch di- to mono--glycosylation. GgCGT is the first di--glycosyltransferase with a crystal structure, and the first -glycosyltransferase with a complex structure containing a sugar acceptor. This work could benefit the development of efficient biocatalysts to synthesize -glycosides with medicinal potential. PubMed: 31986016DOI: 10.1021/jacs.9b12211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.89 Å) |
Structure validation
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