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Insights into the Mechanism of the Antibiotic‐Synthesizing Enzyme MoeO5 from Crystal Structures of Different Complexes
Author(s) -
Ren Feifei,
Ko TzuPing,
Feng Xinxin,
Huang ChunHsiang,
Chan HsiuChien,
Hu Yumei,
Wang Ke,
Ma Yanhe,
Liang PoHuang,
Wang Andrew H.J.,
Oldfield Eric,
Guo ReyTing
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201108002
Subject(s) - triosephosphate isomerase , stereochemistry , barrel (horology) , chemistry , moiety , isomerase , farnesyl pyrophosphate , pyrophosphate , crystallography , enzyme , ligand (biochemistry) , biochemistry , materials science , receptor , atp synthase , composite material
Barrel‐shaped : The enzyme MoeO5 catalyzes the transfer of the C 15 moiety of farnesyl pyrophosphate to the 2‐hydroxy group of 3‐phosphoglycerate to give 2‐( Z , E )‐farnesyl‐3‐phosphoglycerate (FPG; ligand in the center of the shown structure). X‐ray crystallographic structures showed that MoeO5 forms a triose‐phosphate‐isomerase barrel structure and binds FPG in a curved pocket, mainly as a result of its long λ3 loop (magenta in picture).