8E7F

Crystal structure of the autotransporter Ssp from Serratia marcescens.

Summary for 8E7F

• Entry DOI: 10.2210/pdb8e7f/pdb
• Descriptor: Extracellular serine protease, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (6 entities in total)
• Functional Keywords: autotransporter, subtilase, serratia., toxin, hydrolase
• Biological source: Serratia marcescens
• Total number of polymer chains: 1
• Total formula weight: 67342.97

Authors

Hor, L.,Pilapitiya, A.,Panjikar, S.,Paxman, J.J.,Heras, B. (deposition date: 2022-08-23, release date: 2023-03-08, Last modification date: 2024-11-06)

Primary citation

Hor, L.,Pilapitiya, A.,McKenna, J.A.,Panjikar, S.,Anderson, M.A.,Desvaux, M.,Paxman, J.J.,Heras, B.
Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function.
Nat Commun, 14:1163-1163, 2023

PubMed 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.

PubMed: 36859523
DOI: 10.1038/s41467-023-36719-2

Experimental method

X-RAY DIFFRACTION (2 Å)