8GXN

The crystal structure of CsFAOMT2 in complex with SAH

Summary for 8GXN

• Entry DOI: 10.2210/pdb8gxn/pdb
• Descriptor: caffeyl-CoA-O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: csfaomt2, sah, o-methyltransferases, transferase
• Biological source: Theaceae
• Total number of polymer chains: 1
• Total formula weight: 27037.57

Authors

Zhang, Z.M.,Zhou, Y.E.,Huang, H.S. (deposition date: 2022-09-20, release date: 2023-09-20, Last modification date: 2023-11-01)

Primary citation

Jin, J.Q.,Qu, F.R.,Huang, H.,Liu, Q.S.,Wei, M.Y.,Zhou, Y.,Huang, K.L.,Cui, Z.,Chen, J.D.,Dai, W.D.,Zhu, L.,Yao, M.Z.,Zhang, Z.M.,Chen, L.
Characterization of two O-methyltransferases involved in the biosynthesis of O-methylated catechins in tea plant.
Nat Commun, 14:5075-5075, 2023

PubMed Abstract: Tea is known for having a high catechin content, with the main component being (-)-epigallocatechin gallate (EGCG), which has significant bioactivities, including potential anti-cancer and anti-inflammatory activity. The poor intestinal stability and permeability of EGCG, however, undermine these health-improving benefits. O-methylated EGCG derivatives, found in a few tea cultivars in low levels, have attracted considerable interest due to their increased bioavailability. Here, we identify two O-methyltransferases from tea plant: CsFAOMT1 that has a specific O-methyltransferase activity on the 3''-position of EGCG to generate EGCG3''Me, and CsFAOMT2 that predominantly catalyzes the formation of EGCG4″Me. In different tea tissues and germplasms, the transcript levels of CsFAOMT1 and CsFAOMT2 are strongly correlated with the amounts of EGCG3''Me and EGCG4''Me, respectively. Furthermore, the crystal structures of CsFAOMT1 and CsFAOMT2 reveal the key residues necessary for 3''- and 4''-O-methylation. These findings may provide guidance for the future development of tea cultivars with high O-methylated catechin content.

PubMed: 37604798
DOI: 10.1038/s41467-023-40868-9

Experimental method

X-RAY DIFFRACTION (1.34 Å)