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

研究成果: 雜誌貢獻文章同行評審

29 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
289
發行號27
DOIs
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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