Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.
Lipoproteins serve essential roles in the bacterial cell envelope. The posttranslational modification pathway leading to lipoprotein synthesis involves three enzymes. All are potential targets for the development of new antibiotics. Here we report the crystal structure of the last enzyme in the path...
Hlavní autoři: | Wiktor, M, Weichert, D, Howe, N, Huang, C, Olieric, V, Boland, C, Bailey, J, Vogeley, L, Stansfeld, P, Buddelmeijer, N, Wang, M, Caffrey, M |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
Nature Publishing Group
2017
|
Podobné jednotky
-
Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis
Autor: Maciej Wiktor, a další
Vydáno: (2017-07-01) -
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
Autor: Stansfeld, P, a další
Vydáno: (2016) -
Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis
Autor: Samir Olatunji, a další
Vydáno: (2021-07-01) -
Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
Autor: El Ghachi, M, a další
Vydáno: (2018) -
Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development
Autor: Luke Smithers, a další
Vydáno: (2021-12-01)