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.

Bibliographic Details
Main Authors: Sean D. Workman, Liam J. Worrall, Natalie C. J. Strynadka
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
Description
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