Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6LFN

Crystal structure of LpCGTb

Summary for 6LFN
Entry DOI10.2210/pdb6lfn/pdb
DescriptorLpCGTb, PHOSPHATE ION (2 entities in total)
Functional Keywordslpcgtb protein, transferase
Biological sourceLandoltia punctata
Total number of polymer chains2
Total formula weight101171.94
Authors
Gao, H.M.,Yun, C.H. (deposition date: 2019-12-03, release date: 2020-11-18, Last modification date: 2023-11-22)
Primary citationWang, Z.L.,Gao, H.M.,Wang, S.,Zhang, M.,Chen, K.,Zhang, Y.Q.,Wang, H.D.,Han, B.Y.,Xu, L.L.,Song, T.Q.,Yun, C.H.,Qiao, X.,Ye, M.
Dissection of the general two-step di- C -glycosylation pathway for the biosynthesis of (iso)schaftosides in higher plants.
Proc.Natl.Acad.Sci.USA, 117:30816-30823, 2020
Cited by
PubMed Abstract: Schaftoside and isoschaftoside are bioactive natural products widely distributed in higher plants including cereal crops and medicinal herbs. Their biosynthesis may be related with plant defense. However, little is known on the glycosylation biosynthetic pathway of these flavonoid di--glycosides with different sugar residues. Herein, we report that the biosynthesis of (iso)schaftosides is sequentially catalyzed by two -glycosyltransferases (CGTs), i.e., CGTa for -glucosylation of the 2-hydroxyflavanone aglycone and CGTb for -arabinosylation of the mono--glucoside. The two enzymes of the same plant exhibit high homology but remarkably different sugar acceptor and donor selectivities. A total of 14 CGTa and CGTb enzymes were cloned and characterized from seven dicot and monocot plants, including , , ssp. , and , and the in vivo functions for three enzymes were verified by RNA interference and overexpression. Through transcriptome analysis, we found homologous genes in 119 other plants, indicating this pathway is general for the biosynthesis of (iso)schaftosides. Furthermore, we resolved the crystal structures of five CGTs and realized the functional switch of SbCGTb to SbCGTa by structural analysis and mutagenesis of key amino acids. The CGT enzymes discovered in this paper allow efficient synthesis of (iso)schaftosides, and the general glycosylation pathway presents a platform to study the chemical defense mechanisms of higher plants.
PubMed: 33199630
DOI: 10.1073/pnas.2012745117
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.395 Å)
Structure validation

237423

数据于2025-06-11公开中

PDB statisticsPDBj update infoContact PDBjnumon