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The research group of Liu Jinsong, Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, and Zhang Changsheng's research group of the South China Sea Institute of Oceanography, Chinese Academy of Sciences, analyzed the mechanism
of symmetric sugaring of the glycosyltransferase ElaGT in the biosynthesis of Elaiopylin (olive leafin).
The relevant research results are recently titled Substrate-induced dimerization of elaiophylin glycosyltransferase reveals a novel self-activating form of glycosyltransferase for symmetric glycosylation Published in Acta Cryst, an international journal of the Crystallographic Society.
D Struct Biol
.
of symmetric sugaring of the glycosyltransferase ElaGT in the biosynthesis of Elaiopylin (olive leafin).
The relevant research results are recently titled Substrate-induced dimerization of elaiophylin glycosyltransferase reveals a novel self-activating form of glycosyltransferase for symmetric glycosylation Published in Acta Cryst, an international journal of the Crystallographic Society.
D Struct Biol
.
Elaiophilin is a natural macrolide antibiotic containing a 1 6-membered ring with a unique C2 symmetry with a deoxyglycosyl
at each end.
The antibiotic has a novel structure and broad-spectrum antibacterial and antitumor activities, so it has attracted widespread attention
.
ElaGT (elaiophylin glycosyltransferase) is an enzyme responsible for the symmetric transfer of glycans in elaiophylin and is a potential enzymatic tool that expands the structural diversity and activity of Elaiophylin and its analogues.
By analyzing the structure of ElaGT in 4 states, it was found that ElaGT can form a dimer with a coherent channel induced by substrate, the length of which allows an Ela molecule to travel
through the channel.
Further structural analysis and biochemical experiments revealed that the dimer was assembled in a similar way to the mode of action of enzymes and ligands in activator-dependent glycosyltransferases, and its dimer interface could indirectly regulate glycosyl binding sites
.
Thus, the enzyme may employ a self-activated dimer pattern recognition and catalyze glycan transfer
.
This interface interacts with multiple methionines, and mutation of one of which can significantly change the polymerization mode of the enzyme and the ability to bind Ela, which further suggests that the interface is a potential regulatory site
for enzyme activity and substrate specificity.
This study provides new ideas
for exploring the synthesis of analogues with different glycosyl compositions and novel activities by homoglycosyltransferases.
Xu Tingting, associate researcher of Liu Jinsong's research group of Guangzhou Health Institute, and Gan Qingqing, assistant researcher, are the co-first authors of the paper, and researcher Liu Jinsong is the corresponding author
.
The research was supported
by the State Key Laboratory of Respiratory Diseases, the Youth Promotion Association of the Chinese Academy of Sciences, the Guangdong Provincial Key Laboratory of Biomedical Computing, and the Natural Science Foundation of Guangdong Province.
Model diagram of ElaGT self-activated symmetrical sugaring
Article link: https://onlinelibrary.
wiley.
com/doi/full/10.
1107/S2059798322008658?sentby=iucr
