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

Lilian Hor, Akila Pilapitiya, James A. McKenna, Santosh Panjikar, Marilyn A. Anderson, Mickaël Desvaux, Jason J. Paxman () and Begoña Heras ()
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Lilian Hor: La Trobe University
Akila Pilapitiya: La Trobe University
James A. McKenna: La Trobe University
Santosh Panjikar: Australian Synchrotron, ANSTO
Marilyn A. Anderson: La Trobe University
Mickaël Desvaux: INRAE, Université Clermont Auvergne, UMR454 MEDiS
Jason J. Paxman: La Trobe University
Begoña Heras: La Trobe University

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract Autotransporters (ATs) are a large family of bacterial secreted and outer membrane proteins that encompass a wide range of enzymatic activities frequently associated with pathogenic phenotypes. We present the structural and functional characterisation of a subtilase autotransporter, Ssp, from the opportunistic pathogen Serratia marcescens. Although the structures of subtilases have been well documented, this subtilisin-like protein is associated with a 248 residue β-helix and itself includes three finger-like protrusions around its active site involved in substrate interactions. We further reveal that the activity of the subtilase AT is required for entry into epithelial cells as well as causing cellular toxicity. The Ssp structure not only provides details about the subtilase ATs, but also reveals a common framework and function to more distantly related ATs. As such these findings also represent a significant step forward toward understanding the molecular mechanisms underlying the functional divergence in the large AT superfamily.

Date: 2023
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DOI: 10.1038/s41467-023-36719-2

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