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Structure of the catalytic domain of the Salmonella virulence factor SseI

SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting...

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Detalles Bibliográficos
Autores principales: Bhaskaran, Shyam S., Stebbins, C. Erec
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498931/
https://www.ncbi.nlm.nih.gov/pubmed/23151626
http://dx.doi.org/10.1107/S0907444912039042
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author Bhaskaran, Shyam S.
Stebbins, C. Erec
author_facet Bhaskaran, Shyam S.
Stebbins, C. Erec
author_sort Bhaskaran, Shyam S.
collection PubMed
description SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells.
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spelling pubmed-34989312012-11-16 Structure of the catalytic domain of the Salmonella virulence factor SseI Bhaskaran, Shyam S. Stebbins, C. Erec Acta Crystallogr D Biol Crystallogr Research Papers SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells. International Union of Crystallography 2012-11-09 /pmc/articles/PMC3498931/ /pubmed/23151626 http://dx.doi.org/10.1107/S0907444912039042 Text en © Bhaskaran & Stebbins 2012 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Papers
Bhaskaran, Shyam S.
Stebbins, C. Erec
Structure of the catalytic domain of the Salmonella virulence factor SseI
title Structure of the catalytic domain of the Salmonella virulence factor SseI
title_full Structure of the catalytic domain of the Salmonella virulence factor SseI
title_fullStr Structure of the catalytic domain of the Salmonella virulence factor SseI
title_full_unstemmed Structure of the catalytic domain of the Salmonella virulence factor SseI
title_short Structure of the catalytic domain of the Salmonella virulence factor SseI
title_sort structure of the catalytic domain of the salmonella virulence factor ssei
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498931/
https://www.ncbi.nlm.nih.gov/pubmed/23151626
http://dx.doi.org/10.1107/S0907444912039042
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