9GY5

Crystal structure of the catalytic domain from the BoNT-like toxin complex PG1 of Paeniclostridium ghonii

Summary for 9GY5

• Entry DOI: 10.2210/pdb9gy5/pdb
• Descriptor: Catalytic domain from the BoNT-like toxin complex PG1 of Paeniclostridium ghonii, ZINC ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: neurotoxin, metalloprotease, toxin
• Biological source: Paraclostridium ghonii
• Total number of polymer chains: 1
• Total formula weight: 45290.84

Authors

Masuyer, G.,Stenmark, P. (deposition date: 2024-10-01, release date: 2025-10-15, Last modification date: 2025-11-26)

Primary citation

Lee, P.G.,Yin, L.,Wei, X.,Shi, J.,Masuyer, G.,Wentz, T.G.,Chen, P.,Xu, Y.,Liang, J.,Zhang, H.,Persson Kosenina, S.,Lobb, B.,Mansfield, M.,Gill, S.S.,Pellett, S.,Stenmark, P.,Doxey, A.C.,Dong, M.
Identification and characterization of botulinum neurotoxin-like two-component toxins in Paeniclostridium ghonii.
Sci Adv, 11:eadx6145-eadx6145, 2025

PubMed Abstract: Insecticidal bacterial proteins play key roles in insect-bacteria interactions and have been used as biopesticides. Here, we identify two insecticidal proteins in , designated PG-toxin 1 (PG1) and PG-toxin 2 (PG2), which are homologs of botulinum neurotoxins (BoNTs). Unlike BoNTs, PG1 and PG2 contain two separate proteins: One is the protease light chain (LC), and the other is the heavy chain containing the translocation domain and the receptor binding domain. Crystal and cryo-electron microscopy structures show a conserved BoNT-like architecture but without an interchain disulfide bond. Functional characterizations establish that the LCs of PG1 and PG2 cleave insect synaptosomal-associated protein 25 (SNAP25), but not human or rat SNAP25, and microinjection of PG1 and PG2 caused paralysis and death in and mosquitoes. These findings identified unique two-component BoNT-like insecticidal proteins, revealing insights into the evolution of the BoNT family of toxins, and broadening our understanding of bacteria that can be used for biopest controls.

PubMed: 41223264
DOI: 10.1126/sciadv.adx6145

Experimental method

X-RAY DIFFRACTION (1.8 Å)