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

doi:10.1002/anie.201108002

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 journal › Article › peer-review

16 Citations (Scopus)

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 language	English
Pages (from-to)	4157-4160
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	17
DOIs	https://doi.org/10.1002/anie.201108002
Publication status	Published - Apr 23 2012
Externally published	Yes

Keywords

biosynthesis
enzyme catalysis
prenyltransferases
protein folding
protein structures

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201108002

Cite this

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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}",

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doi = "10.1002/anie.201108002",

language = "English",

volume = "51",

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journal = "Angewandte Chemie - International Edition",

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T1 - Insights into the mechanism of the antibiotic-synthesizing enzyme MoeO5 from crystal structures of different complexes

AU - Ren, Feifei

AU - Ko, Tzu Ping

AU - Feng, Xinxin

AU - Huang, Chun Hsiang

AU - Chan, Hsiu Chien

AU - Hu, Yumei

AU - Wang, Ke

AU - Ma, Yanhe

AU - Liang, Po Huang

AU - Wang, Andrew H.J.

AU - Oldfield, Eric

AU - Guo, Rey Ting

PY - 2012/4/23

Y1 - 2012/4/23

N2 - 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).

AB - 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).

KW - biosynthesis

KW - enzyme catalysis

KW - prenyltransferases

KW - protein folding

KW - protein structures

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U2 - 10.1002/anie.201108002

DO - 10.1002/anie.201108002

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

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

Abstract

Keywords

ASJC Scopus subject areas

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