5GHE

Crystal Structure of Bacillus thuringiensis Cry6Aa2 Protoxin

Summary for 5GHE

• Entry DOI: 10.2210/pdb5ghe/pdb
• Descriptor: Pesticidal crystal protein Cry6Aa (2 entities in total)
• Functional Keywords: cry6aa2, clya-type, toxin, bacillus thuringiensis
• Biological source: Bacillus thuringiensis
• Total number of polymer chains: 1
• Total formula weight: 48232.97

Authors

Huang, J.,Guan, Z.,Zou, T.,Sun, M.,Yin, P. (deposition date: 2016-06-19, release date: 2016-08-03, Last modification date: 2024-03-20)

Primary citation

Huang, J.,Guan, Z.,Wan, L.,Zou, T.,Sun, M.
Crystal structure of Cry6Aa: A novel nematicidal ClyA-type alpha-pore-forming toxin from Bacillus thuringiensis
Biochem.Biophys.Res.Commun., 478:307-313, 2016

PubMed Abstract: Crystal (Cry) proteins from Bacillus thuringiensis (Bt) are globally used in agriculture as proteinaceous insecticides. Numerous crystal structures have been determined, and most exhibit conserved three-dimensional architectures. Recently, we have identified a novel nematicidal mechanism by which Cry6Aa triggers cell death through a necrosis-signaling pathway via an interaction with the host protease ASP-1. However, we found little sequence conservation of Cry6Aa in our functional study. Here, we report the 1.90 angstrom (Å) resolution structure of the proteolytic form of Cry6Aa (1-396), determined by X-ray crystallography. The structure of Cry6Aa is highly similar to those of the pathogenic toxin family of ClyA-type α-pore-forming toxins (α-PFTs), which are characterized by a bipartite structure comprising a head domain and a tail domain, thus suggesting that Cry6Aa exhibits a previously undescribed nematicidal mode of action. This structure also provides a framework for the functional study of other nematicidal toxins.

PubMed: 27381865
DOI: 10.1016/j.bbrc.2016.07.002

Experimental method

X-RAY DIFFRACTION (1.901 Å)