Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from escherichia coli

Hsin Yang Chang; Chia Cheng Chou; Min Feng Hsu; Andrew H.J. Wang

doi:10.1074/jbc.M114.575076

Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from escherichia coli

Hsin Yang Chang
, Chia Cheng Chou
, Min Feng Hsu
, Andrew H.J. Wang

醫學科技學院

研究成果: 雜誌貢獻 › 文章 › 同行評審

36 引文斯高帕斯（Scopus）

摘要

Background: UppP, an integral membrane protein involved in the bacterial cell wall synthesis, catalyzes the dephosphorylation of undecaprenyl pyrophosphate. Results: The enzyme active site is proposed by modeling, molecular dynamics, and mutagenesis. Conclusion: The enzyme active-site, composed of (E/Q)XXXE and PGXSRSXXT motifs and a histidine, is proposed to be in the periplasm. Significance: This study provides a first insight into structure-function relationships of E. coli UppP.

原文	英語
頁（從 - 到）	18719-18735
頁數	17
期刊	Journal of Biological Chemistry
卷	289
發行號	27
DOIs	https://doi.org/10.1074/jbc.M114.575076
出版狀態	已發佈 - 7月 4 2014

ASJC Scopus subject areas

生物化學
分子生物學
細胞生物學

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10.1074/jbc.M114.575076

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引用此

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abstract = "Background: UppP, an integral membrane protein involved in the bacterial cell wall synthesis, catalyzes the dephosphorylation of undecaprenyl pyrophosphate. Results: The enzyme active site is proposed by modeling, molecular dynamics, and mutagenesis. Conclusion: The enzyme active-site, composed of (E/Q)XXXE and PGXSRSXXT motifs and a histidine, is proposed to be in the periplasm. Significance: This study provides a first insight into structure-function relationships of E. coli UppP.",

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AU - Chang, Hsin Yang

AU - Chou, Chia Cheng

AU - Hsu, Min Feng

AU - Wang, Andrew H.J.

PY - 2014/7/4

Y1 - 2014/7/4

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AB - Background: UppP, an integral membrane protein involved in the bacterial cell wall synthesis, catalyzes the dephosphorylation of undecaprenyl pyrophosphate. Results: The enzyme active site is proposed by modeling, molecular dynamics, and mutagenesis. Conclusion: The enzyme active-site, composed of (E/Q)XXXE and PGXSRSXXT motifs and a histidine, is proposed to be in the periplasm. Significance: This study provides a first insight into structure-function relationships of E. coli UppP.

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JO - Journal of Biological Chemistry

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ER -

Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from escherichia coli

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ASJC Scopus subject areas

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