Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
Undecaprenyl pyrophosphate phosphatase (UppP) recycles the lipid carrier essential for bacterial cell wall synthesis. Here authors present the crystal structure of UppP from E. coli at 2.0 Å resolution, which sheds light on its phosphatase mechanism and indicates a potential flippase role for UppP.
Main Authors: | , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2018-03-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-03547-8 |
Summary: | Undecaprenyl pyrophosphate phosphatase (UppP) recycles the lipid carrier essential for bacterial cell wall synthesis. Here authors present the crystal structure of UppP from E. coli at 2.0 Å resolution, which sheds light on its phosphatase mechanism and indicates a potential flippase role for UppP. |
---|---|
ISSN: | 2041-1723 |