Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae
The amidotransferase MurT/GatD complex catalyzes peptidoglycan precursor amidation in some Gram-positive bacteria. Here the authors present the crystal structure of the Streptococcus pneumoniae MurT/GatD complex and provide mechanistic insights, which are of interest for drug development.
Main Authors: | Cécile Morlot, Daniel Straume, Katharina Peters, Olav A. Hegnar, Nolwenn Simon, Anne-Marie Villard, Carlos Contreras-Martel, Francisco Leisico, Eefjan Breukink, Christine Gravier-Pelletier, Laurent Le Corre, Waldemar Vollmer, Nicolas Pietrancosta, Leiv Sigve Håvarstein, André Zapun |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2018-08-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-05602-w |
Similar Items
-
Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus.
by: Daniela Münch, et al.
Published: (2012-01-01) -
OsGatB, the subunit of tRNA-dependent amidotransferase, is required for primary root development in rice
by: Cheng eQin, et al.
Published: (2016-05-01) -
Fluorescence anisotropy assays for high throughput screening of compounds binding to lipid II, PBP1b, FtsW and MurJ
by: Adrien Boes, et al.
Published: (2020-04-01) -
Characterization of Arabidopsis glutamine PRPP amidotransferase-deficient mutants
by: Wei-Fon Hung, et al.
Published: (2004) -
CRISPR Interference for Rapid Knockdown of Essential Cell Cycle Genes in Lactobacillus plantarum
by: Ine Storaker Myrbråten, et al.
Published: (2019-03-01)