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¹H, ¹³C, and ¹⁵N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis.

ABSTRACT: 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.

SUBMITTER: Davis JL

PROVIDER: S-EPMC9510096 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

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1H, 13C, and 15N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis.

Davis Jessica L JL Hounslow Andrea M AM Baxter Nicola J NJ Mesnage Stéphane S Williamson Mike P MP Williamson Mike P MP

Biomolecular NMR assignments 20220604 2

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 a ...[more]

PMID: 35665899

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