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

18 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\}",

year = "2012",

month = apr,

day = "23",

doi = "10.1002/anie.201108002",

language = "English",

volume = "51",

pages = "4157--4160",

journal = "Angewandte Chemie - International Edition",

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publisher = "John Wiley and Sons Ltd",

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TY - JOUR

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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UR - https://www.scopus.com/pages/publications/84859940094#tab=citedBy

U2 - 10.1002/anie.201108002

DO - 10.1002/anie.201108002

M3 - Article

C2 - 22431288

AN - SCOPUS:84859940094

SN - 1433-7851

VL - 51

SP - 4157

EP - 4160

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 17

ER -

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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