Insights into the mechanism of the antibiotic-synthesizing enzyme MoeO5 from crystal structures of different complexes

Feifei Ren, Tzu Ping Ko, Xinxin Feng, Chun Hsiang Huang, Hsiu Chien Chan, Yumei Hu, Ke Wang, Yanhe Ma, Po Huang Liang, Andrew H.J. Wang, Eric Oldfield, Rey Ting Guo

Research output: Contribution to journalArticlepeer-review

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).

Original languageEnglish (US)
Pages (from-to)4157-4160
Number of pages4
JournalAngewandte Chemie - International Edition
Volume51
Issue number17
DOIs
StatePublished - Apr 23 2012

Keywords

  • biosynthesis
  • enzyme catalysis
  • prenyltransferases
  • protein folding
  • protein structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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