5GL5
Sterol 3-beta-glucosyltransferase (ugt51) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c): UDPG complex
Summary for 5GL5
| Entry DOI | 10.2210/pdb5gl5/pdb |
| Descriptor | Sterol 3-beta-glucosyltransferase, URIDINE-5'-DIPHOSPHATE-GLUCOSE (3 entities in total) |
| Functional Keywords | glycotransferase, complex, native, transferase |
| Biological source | Saccharomyces cerevisiae S288c (yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 113134.79 |
| Authors | Feng, Y.,Chen, L.-Q. (deposition date: 2016-07-08, release date: 2017-01-11, Last modification date: 2023-11-08) |
| Primary citation | Chen, L.-Q.,Zhang, Y.,Feng, Y. Structural Dissection of Sterol Glycosyltransferase UGT51 from Saccharomyces cerevisiae for Substrate Specificity. J. Struct. Biol., 2018 Cited by PubMed Abstract: Sterol glycosyltransferases catalyze the formation of a variety of glycosylated sterol derivatives and are involved in producing a plethora of bioactive natural products. To understand the molecular mechanism of sterol glycosyltransferases, we determined crystal structures of a sterol glycosyltransferase UGT51 from Saccharomyces cerevisiae. The structures of the UGT51 and its complex with uridine diphosphate glucose (UDPG) were solved at resolutions of 2.77 Å and 1.9 Å, respectively. The structural analysis revealed that a long hydrophobic cavity, 9.2 Å in width and 17.6 Å in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. Furthermore, a short, conserved sequence of S847-M851 was identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations indicated that changed unique interaction network in mutant M7_1 (SA/LA/VA/KA/EK/SA/ND), with an 1800-fold activity improvement toward an unnatural substrate protopanaxadiol (PPD), might influence its substrate preference. This study reported the first sterol glycosyltransferase structure, providing a molecular blueprint for generating tailored sterol glycosyltransferases as potential catalytic elements in synthetic biology. PubMed: 30395931DOI: 10.1016/j.jsb.2018.11.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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