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Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa
Peptidoglycan (PG) is an essential component of the bacterial cell wall and is assembled from a lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed in particular by bifunctional class A penicillin-binding proteins (aPBPs). In the major clinical pathogen Pseudomonas aerug...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7267771/ https://www.ncbi.nlm.nih.gov/pubmed/32320673 http://dx.doi.org/10.1016/j.str.2020.03.012 |
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author | Caveney, Nathanael A. Egan, Alexander J.F. Ayala, Isabel Laguri, Cédric Robb, Craig S. Breukink, Eefjan Vollmer, Waldemar Strynadka, Natalie C.J. Simorre, Jean-Pierre |
author_facet | Caveney, Nathanael A. Egan, Alexander J.F. Ayala, Isabel Laguri, Cédric Robb, Craig S. Breukink, Eefjan Vollmer, Waldemar Strynadka, Natalie C.J. Simorre, Jean-Pierre |
author_sort | Caveney, Nathanael A. |
collection | PubMed |
description | Peptidoglycan (PG) is an essential component of the bacterial cell wall and is assembled from a lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed in particular by bifunctional class A penicillin-binding proteins (aPBPs). In the major clinical pathogen Pseudomonas aeruginosa, PBP1B is anchored within the cytoplasmic membrane but regulated by a bespoke outer membrane-localized lipoprotein known as LpoP. Here, we report the structure of LpoP, showing an extended N-terminal, flexible tether followed by a well-ordered C-terminal tandem-tetratricopeptide repeat domain. We show that LpoP stimulates both PBP1B transpeptidase and glycosyltransferase activities in vitro and interacts directly via its C terminus globular domain with the central UB2H domain of PBP1B. Contrary to the situation in E. coli, P. aeruginosa CpoB does not regulate PBP1B/LpoP in vitro. We propose a mechanism that helps to underscore similarities and differences in class A PBP activation across Gram-negative bacteria. |
format | Online Article Text |
id | pubmed-7267771 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-72677712020-06-08 Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa Caveney, Nathanael A. Egan, Alexander J.F. Ayala, Isabel Laguri, Cédric Robb, Craig S. Breukink, Eefjan Vollmer, Waldemar Strynadka, Natalie C.J. Simorre, Jean-Pierre Structure Article Peptidoglycan (PG) is an essential component of the bacterial cell wall and is assembled from a lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed in particular by bifunctional class A penicillin-binding proteins (aPBPs). In the major clinical pathogen Pseudomonas aeruginosa, PBP1B is anchored within the cytoplasmic membrane but regulated by a bespoke outer membrane-localized lipoprotein known as LpoP. Here, we report the structure of LpoP, showing an extended N-terminal, flexible tether followed by a well-ordered C-terminal tandem-tetratricopeptide repeat domain. We show that LpoP stimulates both PBP1B transpeptidase and glycosyltransferase activities in vitro and interacts directly via its C terminus globular domain with the central UB2H domain of PBP1B. Contrary to the situation in E. coli, P. aeruginosa CpoB does not regulate PBP1B/LpoP in vitro. We propose a mechanism that helps to underscore similarities and differences in class A PBP activation across Gram-negative bacteria. Cell Press 2020-06-02 /pmc/articles/PMC7267771/ /pubmed/32320673 http://dx.doi.org/10.1016/j.str.2020.03.012 Text en © 2020 The Authors http://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 | Article Caveney, Nathanael A. Egan, Alexander J.F. Ayala, Isabel Laguri, Cédric Robb, Craig S. Breukink, Eefjan Vollmer, Waldemar Strynadka, Natalie C.J. Simorre, Jean-Pierre Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title | Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title_full | Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title_fullStr | Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title_full_unstemmed | Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title_short | Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa |
title_sort | structure of the peptidoglycan synthase activator lpop in pseudomonas aeruginosa |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7267771/ https://www.ncbi.nlm.nih.gov/pubmed/32320673 http://dx.doi.org/10.1016/j.str.2020.03.012 |
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