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

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 pept...

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Autores principales: Davis, Jessica L., Hounslow, Andrea M., Baxter, Nicola J., Mesnage, Stéphane, Williamson, Mike P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510096/
https://www.ncbi.nlm.nih.gov/pubmed/35665899
http://dx.doi.org/10.1007/s12104-022-10087-2
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author Davis, Jessica L.
Hounslow, Andrea M.
Baxter, Nicola J.
Mesnage, Stéphane
Williamson, Mike P.
author_facet Davis, Jessica L.
Hounslow, Andrea M.
Baxter, Nicola J.
Mesnage, Stéphane
Williamson, Mike P.
author_sort Davis, Jessica L.
collection PubMed
description 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.
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spelling pubmed-95100962022-09-27 (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis Davis, Jessica L. Hounslow, Andrea M. Baxter, Nicola J. Mesnage, Stéphane Williamson, Mike P. Biomol NMR Assign Article 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. Springer Netherlands 2022-06-04 2022 /pmc/articles/PMC9510096/ /pubmed/35665899 http://dx.doi.org/10.1007/s12104-022-10087-2 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/ Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Davis, Jessica L.
Hounslow, Andrea M.
Baxter, Nicola J.
Mesnage, Stéphane
Williamson, Mike P.
(1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title_full (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title_fullStr (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title_full_unstemmed (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title_short (1)H, (13)C, and (15)N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
title_sort (1)h, (13)c, and (15)n resonance assignments of a conserved putative cell wall binding domain from enterococcus faecalis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510096/
https://www.ncbi.nlm.nih.gov/pubmed/35665899
http://dx.doi.org/10.1007/s12104-022-10087-2
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