Structure and activation mechanism of the Makes caterpillars floppy 1 toxin

Alexander Belyy, Philipp Heilen, Philine Hagel, Oliver Hofnagel and Stefan Raunser ()
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Alexander Belyy: Max Planck Institute of Molecular Physiology
Philipp Heilen: Max Planck Institute of Molecular Physiology
Philine Hagel: Max Planck Institute of Molecular Physiology
Oliver Hofnagel: Max Planck Institute of Molecular Physiology
Stefan Raunser: Max Planck Institute of Molecular Physiology

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract The bacterial Makes caterpillars floppy 1 (Mcf1) toxin promotes apoptosis in insects, leading to loss of body turgor and death. The molecular mechanism underlying Mcf1 intoxication is poorly understood. Here, we present the cryo-EM structure of Mcf1 from Photorhabdus luminescens, revealing a seahorse-like shape with a head and tail. While the three head domains contain two effectors, as well as an activator-binding domain (ABD) and an autoprotease, the tail consists of two putative translocation and three putative receptor-binding domains. Rearrangement of the tail moves the C-terminus away from the ABD and allows binding of the host cell ADP-ribosylation factor 3, inducing conformational changes that position the cleavage site closer to the protease. This distinct activation mechanism that is based on a hook-loop interaction results in three autocleavage reactions and the release of two toxic effectors. Unexpectedly, the BH3-like domain containing ABD is not an active effector. Our findings allow us to understand key steps of Mcf1 intoxication at the molecular level.

Date: 2023
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DOI: 10.1038/s41467-023-44069-2

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