6INF

a glycosyltransferase complex with UDP

Summary for 6INF

• Entry DOI: 10.2210/pdb6inf/pdb
• Descriptor: UDP-glycosyltransferase 76G1, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: complex, transferase
• Biological source: Stevia rebaudiana (Stevia)
• Total number of polymer chains: 1
• Total formula weight: 53562.39

Authors

Zhu, X.,Yang, T.,Naismith, J.H. (deposition date: 2018-10-25, release date: 2019-07-31, Last modification date: 2023-11-22)

Primary citation

Yang, T.,Zhang, J.,Ke, D.,Yang, W.,Tang, M.,Jiang, J.,Cheng, G.,Li, J.,Cheng, W.,Wei, Y.,Li, Q.,Naismith, J.H.,Zhu, X.
Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations.
Nat Commun, 10:3214-3214, 2019

PubMed Abstract: Diets high in sugar are recognized as a serious health problem, and there is a drive to reduce their consumption. Steviol glycosides are natural zero-calorie sweeteners, but the most desirable ones are biosynthesized with low yields. UGT76G1 catalyzes the β (1-3) addition of glucose to steviol glycosides, which gives them the preferred taste. UGT76G1 is able to transfer glucose to multiple steviol substrates yet remains highly specific in the glycosidic linkage it creates. Here, we report multiple complex structures of the enzyme combined with biochemical data, which reveal that the enzyme utilizes hydrophobic interactions for substrate recognition. The lack of a strict three-dimensional recognition arrangement, typical of hydrogen bonds, permits two different orientations for β (1-3) sugar addition. The use of hydrophobic recognition is unusual in a regio- and stereo-specific catalysis. Harnessing such non-specific hydrophobic interactions could have wide applications in the synthesis of complex glycoconjugates.

PubMed: 31324778
DOI: 10.1038/s41467-019-11154-4

Experimental method

X-RAY DIFFRACTION (1.69 Å)