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Bioinformatic analysis of WxL domain proteins

The WxL domain is found on the cell surface of many bacteria, most of which are commensal gut bacteria. Its functions are generally identified as being related to virulence and/or peptidoglycan attachment, but there is so far no clear function or structure for this domain. Here, a range of bioinform...

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Detalles Bibliográficos
Autores principales: Hassan, Mahreen U., Williamson, Mike P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9772566/
https://www.ncbi.nlm.nih.gov/pubmed/36568411
http://dx.doi.org/10.1016/j.sjbs.2022.103526
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author Hassan, Mahreen U.
Williamson, Mike P.
author_facet Hassan, Mahreen U.
Williamson, Mike P.
author_sort Hassan, Mahreen U.
collection PubMed
description The WxL domain is found on the cell surface of many bacteria, most of which are commensal gut bacteria. Its functions are generally identified as being related to virulence and/or peptidoglycan attachment, but there is so far no clear function or structure for this domain. Here, a range of bioinformatics tools were used to clarify the structure and function. These indicate that WxL domains occur in cell surface-associated gene clusters that always contain a small WxL, large WxL and DUF916 domain; and that the small and large WxL proteins have distinct structure despite sharing two conserved WxL motifs. The two WxL motifs form a hydrophobic surface buried inside the protein. The likely function of the WxL domain is to attach to bacterial peptidoglycan, forming a platform to allow associated domains in the cluster to interact with host proteins.
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spelling pubmed-97725662022-12-23 Bioinformatic analysis of WxL domain proteins Hassan, Mahreen U. Williamson, Mike P. Saudi J Biol Sci Original Article The WxL domain is found on the cell surface of many bacteria, most of which are commensal gut bacteria. Its functions are generally identified as being related to virulence and/or peptidoglycan attachment, but there is so far no clear function or structure for this domain. Here, a range of bioinformatics tools were used to clarify the structure and function. These indicate that WxL domains occur in cell surface-associated gene clusters that always contain a small WxL, large WxL and DUF916 domain; and that the small and large WxL proteins have distinct structure despite sharing two conserved WxL motifs. The two WxL motifs form a hydrophobic surface buried inside the protein. The likely function of the WxL domain is to attach to bacterial peptidoglycan, forming a platform to allow associated domains in the cluster to interact with host proteins. Elsevier 2023-02 2022-12-07 /pmc/articles/PMC9772566/ /pubmed/36568411 http://dx.doi.org/10.1016/j.sjbs.2022.103526 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Original Article
Hassan, Mahreen U.
Williamson, Mike P.
Bioinformatic analysis of WxL domain proteins
title Bioinformatic analysis of WxL domain proteins
title_full Bioinformatic analysis of WxL domain proteins
title_fullStr Bioinformatic analysis of WxL domain proteins
title_full_unstemmed Bioinformatic analysis of WxL domain proteins
title_short Bioinformatic analysis of WxL domain proteins
title_sort bioinformatic analysis of wxl domain proteins
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9772566/
https://www.ncbi.nlm.nih.gov/pubmed/36568411
http://dx.doi.org/10.1016/j.sjbs.2022.103526
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