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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

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.

Original languageEnglish
Pages (from-to)18719-18735
Number of pages17
JournalJournal of Biological Chemistry
Volume289
Issue number27
DOIs
StatePublished - 4 Jul 2014

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