TY - JOUR
T1 - Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from escherichia coli
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
N2 - 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.
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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U2 - 10.1074/jbc.M114.575076
DO - 10.1074/jbc.M114.575076
M3 - Article
C2 - 24855653
AN - SCOPUS:84903844156
SN - 0021-9258
VL - 289
SP - 18719
EP - 18735
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 27
ER -