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 language | English |
|---|---|
| Pages (from-to) | 18719-18735 |
| Number of pages | 17 |
| Journal | Journal of Biological Chemistry |
| Volume | 289 |
| Issue number | 27 |
| DOIs | |
| Publication status | Published - Jul 4 2014 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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