Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function

Autotransporters are bacterial proteins that possess multiple activities associated with pathogenesis. Here the authors present the structure of the autotransporter subtilase Ssp from Serratia marcescens and show that its distinctive structural features are required for its cytotoxic function.

Bibliographic Details
Main Authors: Lilian Hor, Akila Pilapitiya, James A. McKenna, Santosh Panjikar, Marilyn A. Anderson, Mickaël Desvaux, Jason J. Paxman, Begoña Heras
Format: Article
Language:English
Published: Nature Portfolio 2023-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-023-36719-2
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author Lilian Hor
Akila Pilapitiya
James A. McKenna
Santosh Panjikar
Marilyn A. Anderson
Mickaël Desvaux
Jason J. Paxman
Begoña Heras
author_facet Lilian Hor
Akila Pilapitiya
James A. McKenna
Santosh Panjikar
Marilyn A. Anderson
Mickaël Desvaux
Jason J. Paxman
Begoña Heras
author_sort Lilian Hor
collection DOAJ
description Autotransporters are bacterial proteins that possess multiple activities associated with pathogenesis. Here the authors present the structure of the autotransporter subtilase Ssp from Serratia marcescens and show that its distinctive structural features are required for its cytotoxic function.
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spelling doaj.art-92aa96900898463092e56bee5126bdf02023-03-22T11:45:28ZengNature PortfolioNature Communications2041-17232023-03-0114111310.1038/s41467-023-36719-2Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic functionLilian Hor0Akila Pilapitiya1James A. McKenna2Santosh Panjikar3Marilyn A. Anderson4Mickaël Desvaux5Jason J. Paxman6Begoña Heras7Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityAustralian Synchrotron, ANSTODepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityINRAE, Université Clermont Auvergne, UMR454 MEDiSDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityDepartment of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, La Trobe UniversityAutotransporters are bacterial proteins that possess multiple activities associated with pathogenesis. Here the authors present the structure of the autotransporter subtilase Ssp from Serratia marcescens and show that its distinctive structural features are required for its cytotoxic function.https://doi.org/10.1038/s41467-023-36719-2
spellingShingle Lilian Hor
Akila Pilapitiya
James A. McKenna
Santosh Panjikar
Marilyn A. Anderson
Mickaël Desvaux
Jason J. Paxman
Begoña Heras
Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
Nature Communications
title Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
title_full Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
title_fullStr Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
title_full_unstemmed Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
title_short Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
title_sort crystal structure of a subtilisin like autotransporter passenger domain reveals insights into its cytotoxic function
url https://doi.org/10.1038/s41467-023-36719-2
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