1 H, 13 C, and 15 N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis.
Jessica L DavisAndrea M HounslowNicola J BaxterMichael P WilliamsonStéphane MesnagePublished in: Biomolecular NMR assignments (2022)
Enterococcus faecalis is a major causative agent of hospital acquired infections. The ability of E. faecalis to evade the host immune system is essential during pathogenesis, which has been shown to be dependent on the complete separation of daughter cells by peptidoglycan hydrolases. AtlE is a peptidoglycan hydrolase which is predicted to bind to the cell wall of E. faecalis, via six C-terminal repeat sequences. Here, we report the near complete assignment of one of these six repeats, as well as the predicted backbone structure and dynamics. This data will provide a platform for future NMR studies to explore the ligand recognition motif of AtlE and help to uncover its potential role in E. faecalis virulence.
Keyphrases
- cell wall
- induced apoptosis
- cell cycle arrest
- escherichia coli
- pseudomonas aeruginosa
- magnetic resonance
- staphylococcus aureus
- healthcare
- transcription factor
- electronic health record
- high throughput
- biofilm formation
- current status
- machine learning
- case control
- endoplasmic reticulum stress
- liquid chromatography
- cell death
- acute care
- binding protein
- deep learning
- cell proliferation
- single cell
- pi k akt
- genetic diversity