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I03-Macromolecular Crystallography	14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface Tobias Karlberg , Peter Hornyak , Ana Filipa Pinto , Stefina Milanova , Mahsa Ebrahimi , Mikael Lindberg , Nikolai Püllen , Axel Nordström , Elinor Löverli , Rémi Caraballo , Emily V. Wong , Katja Näreoja , Ann-gerd Thorsell , Mikael Elofsson , Enrique M. De La Cruz , Camilla Björkegren , Herwig Schüler Nature Communications 9 DOI: 10.1038/s41467-018-06194-1 Diamond Proposal Number(s): [11265, 15806] Open Access Show Abstract ▼ Abstract: Pseudomonas are a common cause of hospital-acquired infections that may be lethal. ADP-ribosyltransferase activities of Pseudomonas exotoxin-S and -T depend on 14-3-3 proteins inside the host cell. By binding in the 14-3-3 phosphopeptide binding groove, an amphipathic C-terminal helix of ExoS and ExoT has been thought to be crucial for their activation. However, crystal structures of the 14-3-3β:ExoS and -ExoT complexes presented here reveal an extensive hydrophobic interface that is sufficient for complex formation and toxin activation. We show that C-terminally truncated ExoS ADP-ribosyltransferase domain lacking the amphipathic binding motif is active when co-expressed with 14-3-3. Moreover, swapping the amphipathic C-terminus with a fragment from Vibrio Vis toxin creates a 14-3-3 independent toxin that ADP-ribosylates known ExoS targets. Finally, we show that 14-3-3 stabilizes ExoS against thermal aggregation. Together, this indicates that 14-3-3 proteins activate exotoxin ADP-ribosyltransferase domains by chaperoning their hydrophobic surfaces independently of the amphipathic C-terminal segment.	Sep 2018

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I03-Macromolecular Crystallography

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface