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Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA

Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure...

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Autores principales: Ghequire, Maarten G. K., Garcia-Pino, Abel, Lebbe, Eline K. M., Spaepen, Stijn, Loris, Remy, De Mot, René
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585409/
https://www.ncbi.nlm.nih.gov/pubmed/23468636
http://dx.doi.org/10.1371/journal.ppat.1003199
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author Ghequire, Maarten G. K.
Garcia-Pino, Abel
Lebbe, Eline K. M.
Spaepen, Stijn
Loris, Remy
De Mot, René
author_facet Ghequire, Maarten G. K.
Garcia-Pino, Abel
Lebbe, Eline K. M.
Spaepen, Stijn
Loris, Remy
De Mot, René
author_sort Ghequire, Maarten G. K.
collection PubMed
description Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure of LlpA(BW), the prototype lectin-like bacteriocin from Pseudomonas putida, reveals an architecture of two monocot mannose-binding lectin (MMBL) domains and a C-terminal β-hairpin extension. The C-terminal MMBL domain (C-domain) adopts a fold very similar to MMBL domains from plant lectins and contains a binding site for mannose and oligomannosides. Mutational analysis indicates that an intact sugar-binding pocket in this domain is crucial for bactericidal activity. The N-terminal MMBL domain (N-domain) adopts the same fold but is structurally more divergent and lacks a functional mannose-binding site. Differential activity of engineered N/C-domain chimers derived from two LlpA homologues with different killing spectra, disclosed that the N-domain determines target specificity. Apparently this bacteriocin is assembled from two structurally similar domains that evolved separately towards dedicated functions in target recognition and bacteriotoxicity.
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spelling pubmed-35854092013-03-06 Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA Ghequire, Maarten G. K. Garcia-Pino, Abel Lebbe, Eline K. M. Spaepen, Stijn Loris, Remy De Mot, René PLoS Pathog Research Article Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure of LlpA(BW), the prototype lectin-like bacteriocin from Pseudomonas putida, reveals an architecture of two monocot mannose-binding lectin (MMBL) domains and a C-terminal β-hairpin extension. The C-terminal MMBL domain (C-domain) adopts a fold very similar to MMBL domains from plant lectins and contains a binding site for mannose and oligomannosides. Mutational analysis indicates that an intact sugar-binding pocket in this domain is crucial for bactericidal activity. The N-terminal MMBL domain (N-domain) adopts the same fold but is structurally more divergent and lacks a functional mannose-binding site. Differential activity of engineered N/C-domain chimers derived from two LlpA homologues with different killing spectra, disclosed that the N-domain determines target specificity. Apparently this bacteriocin is assembled from two structurally similar domains that evolved separately towards dedicated functions in target recognition and bacteriotoxicity. Public Library of Science 2013-02-28 /pmc/articles/PMC3585409/ /pubmed/23468636 http://dx.doi.org/10.1371/journal.ppat.1003199 Text en © 2013 Ghequire et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ghequire, Maarten G. K.
Garcia-Pino, Abel
Lebbe, Eline K. M.
Spaepen, Stijn
Loris, Remy
De Mot, René
Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title_full Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title_fullStr Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title_full_unstemmed Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title_short Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA
title_sort structural determinants for activity and specificity of the bacterial toxin llpa
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585409/
https://www.ncbi.nlm.nih.gov/pubmed/23468636
http://dx.doi.org/10.1371/journal.ppat.1003199
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