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...
Autors principals: | Wiktor, M, Weichert, D, Howe, N, Huang, C, Olieric, V, Boland, C, Bailey, J, Vogeley, L, Stansfeld, P, Buddelmeijer, N, Wang, M, Caffrey, M |
---|---|
Format: | Journal article |
Idioma: | English |
Publicat: |
Nature Publishing Group
2017
|
Ítems similars
-
Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis
per: Maciej Wiktor, et al.
Publicat: (2017-07-01) -
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
per: Stansfeld, P, et al.
Publicat: (2016) -
Structural basis of the membrane intramolecular transacylase reaction responsible for lyso-form lipoprotein synthesis
per: Samir Olatunji, et al.
Publicat: (2021-07-01) -
Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
per: El Ghachi, M, et al.
Publicat: (2018) -
Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development
per: Luke Smithers, et al.
Publicat: (2021-12-01)