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8K08

Pq3-O-UGT2 with 20(S)-Ginsenoside Rh2

Summary for 8K08
Entry DOI10.2210/pdb8k08/pdb
DescriptorGlycosyltransferase, Ginsenoside Rh2 (2 entities in total)
Functional Keywordsglycosytransferase, transferase
Biological sourcePanax quinquefolius
Total number of polymer chains2
Total formula weight103021.85
Authors
Ji, Q.S.,Liu, Y.R.,Mei, K.R. (deposition date: 2023-07-07, release date: 2025-01-29, Last modification date: 2025-02-12)
Primary citationJi, Q.,Liu, Y.,Zhang, H.,Gao, Y.,Ding, Y.,Ding, Y.,Xie, J.,Zhang, J.,Jin, X.,Lai, B.,Chen, C.,Wang, J.,Gao, W.,Mei, K.
Structural Insights into the Substrate Recognition of Ginsenoside Glycosyltransferase Pq3-O-UGT2.
Adv Sci, :e2413185-e2413185, 2025
Cited by
PubMed Abstract: Ginsenosides are a group of tetracyclic triterpenoids with promising health benefits, consisting of ginseng aglycone attached to various glycans. Pq3-O-UGT2, an important UDP-dependent glycosyltransferase (UGT), catalyzes the production of Ginsenoside Rg3 and Rd by extending the glycan chain of Ginsenoside Rh2 and F2, respectively, with higher selectivity for F2. However, the mechanism underlying its substrate recognition remains unclear. In this study, the crystal structures of Pq3-O-UGT2 in complex with its acceptor substrates are solved. The structures revealed a Nα5-oriented acceptor binding pocket in Pq3-O-UGT2, shaped by the unique conformation of the Nα5-Nα6 linker. Hydrophobic interactions play a pivotal role in the recognition of both Rh2 and F2, while hydrogen bonds specifically aid in F2 recognition due to its additional glucose moiety. The hydrophobic nature of the acceptor binding pocket also enables Pq3-O-UGT2 to recognize flavonoids. Overall, this study provides novel insights into the substrate recognition mechanisms of ginsenoside UGTs, advancing the understanding of their function and specificity.
PubMed: 39887940
DOI: 10.1002/advs.202413185
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

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