Davis, J.L., Hounslow, A.M., Baxter, N.J. et al. (2 more authors) (2022) 1H, 13C, and 15N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis. Biomolecular NMR Assignments, 16. pp. 247-251. ISSN 1874-2718
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2022 The Authors. This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
Keywords: | Peptidoglycan; Hydrolase; E. faecalis; AtlE; R6 |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) |
Funding Information: | Funder Grant number Biotechnology and Biological Sciences Research Council 2283067 |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 03 Nov 2022 11:34 |
Last Modified: | 10 Feb 2023 14:14 |
Status: | Published |
Publisher: | Springer |
Refereed: | Yes |
Identification Number: | 10.1007/s12104-022-10087-2 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:192932 |