@article{579aa17a514a44389cddc99785f434ec,
title = "Insights into the mechanism of the antibiotic-synthesizing enzyme MoeO5 from crystal structures of different complexes",
abstract = "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).",
keywords = "biosynthesis, enzyme catalysis, prenyltransferases, protein folding, protein structures",
author = "Feifei Ren and Ko, {Tzu Ping} and Xinxin Feng and Huang, {Chun Hsiang} and Chan, {Hsiu Chien} and Yumei Hu and Ke Wang and Yanhe Ma and Liang, {Po Huang} and Wang, {Andrew H.J.} and Eric Oldfield and Guo, {Rey Ting}",
year = "2012",
month = apr,
day = "23",
doi = "10.1002/anie.201108002",
language = "English",
volume = "51",
pages = "4157--4160",
journal = "Angewandte Chemie - International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "17",
}