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4PKM

Crystal Structure of Bacillus thuringiensis Cry51Aa1 Protoxin at 1.65 Angstroms Resolution

Summary for 4PKM
Entry DOI10.2210/pdb4pkm/pdb
DescriptorCry51Aa1, GLYCEROL, SULFATE ION, ... (5 entities in total)
Functional Keywordsbacterial toxins, cry toxins, pore-forming toxins, beta-pore-forming toxins, beetles, insecticidal toxins, pro-toxins, toxin
Biological sourceBacillus thuringiensis
Total number of polymer chains1
Total formula weight34420.19
Authors
Xu, C.,Chinte, U.,Chen, L.,Yao, Q.,Zhou, D.,Meng, Y.,Li, L.,Rose, J.,Bi, L.J.,Yu, Z.,Sun, M.,Wang, B.C. (deposition date: 2014-05-15, release date: 2015-06-03, Last modification date: 2023-12-27)
Primary citationXu, C.,Chinte, U.,Chen, L.,Yao, Q.,Meng, Y.,Zhou, D.,Bi, L.J.,Rose, J.,Adang, M.J.,Wang, B.C.,Yu, Z.,Sun, M.
Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type beta-pore-forming toxin from Bacillus thuringiensis.
Biochem.Biophys.Res.Commun., 462:184-189, 2015
Cited by
PubMed Abstract: The structures of several Bacillus thuringiensis (Bt) insecticidal crystal proteins have been determined by crystallographic methods and a close relationship has been explicated between specific toxicities and conserved three-dimensional architectures. In this study, as a representative of the coleopteran- and hemipteran-specific Cry51A group, the complete structure of Cry51Aa1 protoxin has been determined by X-ray crystallography at 1.65 Å resolution. This is the first report of a coleopteran-active Bt insecticidal toxin with high structural similarity to the aerolysin-type β-pore forming toxins (β-PFTs). Moreover, study of featured residues and structural elements reveal their possible roles in receptor binding and pore formation events. This study provides new insights into the action of aerolysin-type β-PFTs from a structural perspective, and could be useful for the control of coleopteran and hemipteran insect pests in agricultures.
PubMed: 25957471
DOI: 10.1016/j.bbrc.2015.04.068
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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