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Genetic element
(GENE)
last updated: 02 Feb 2023
Vpb4Da2
EN
-
Vip4Da2EN
CS-vpb4da2-BACTU
EN
Protein coding sequence
No
-
BCH-ORGA-SCBD-45614-11 Organism Bacillus thuringiensis (Bt, Bacillus, BACTU)Bacteria
Bacillus thuringiensis stain EG6657
EN
The VPD4Da2 protein has a similar mode of action to other Bt proteins: proteolytic activation, binding to a receptor in the midgut, oligomerization in the membrane, pore formation and cell death. This cellular damage leads to death of the insect. However, the protein forms beta-barrel pores rather than the alpha-helical transmembrane pores Bt proteins form.
EN
The Vpb4Da2 structure depicts an overall architecture of six structural domains:
- Domain 1 (amino acids 1–263), which encompasses a characteristic PA14 domain, adopts a conformation of ten anti-parallel β-strands, six small α-helices, and binds two adjacent calcium ions visible in the structure
- Domain 2 (amino acids 264–483) consists of a β-hairpin motif, seven anti-parallel β-strands, a partially structured long loop, and three additional α-helices.
- Domain 3 (amino acids 484–593) has a β-sandwich fold of seven β-strands and four α-helices.
- Domain 4 (amino acids 594–730) consists of β-strands exhibiting a classical β-jelly roll fold and harboring a calcium ion.
- Domain 5 (amino acids 731–820) has an immunoglobulin-like fold of six β-strands and one α-helix.
- Domain 6 (amino acids 821–937), like domain 5, adopts an immunoglobulin-like fold with seven β-strands and two α-helices.
- A new Bacillus thuringiensis protein for Western corn rootworm control.pdf [ English ]
- Structural and functional insights into the first Bacillus thuringiensis vegetative insecticidal protein of the Vpb4 fold, active against western corn rootworm.pdf [ English ]
- Food and feed safety of the Bacillus thuringiensis derived protein Vpb4Da2, a novel protein for control of western corn rootworm.pdf [ English ]
- GenBank - Synthetic construct Vip4Da2 gene, complete cds [ English ]
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