PDBsum entry 6v1v

Toxin

PDB id: 6v1v

Contents

Protein chains

752 a.a.

PDB id:

6v1v

Name:

Toxin

Title:

Vip3b (vip3b_2160) adapted for crystallization

Structure:

Vegetative insecticidal protein. Chain: a, b, c, d. Synonym: vip3b2160. Engineered: yes. Mutation: yes

Source:

Bacillus thuringiensis. Organism_taxid: 1428. Gene: vip3bc1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: ripl.

Resolution:

3.19Å R-factor: 0.218 R-free: 0.259

Authors:

A.G.Evdokimov,M.Zheng,F.Moshiri,J.Haas,C.Lowder

Key ref:

M.Zheng et al. (2020). Crystal structure of a Vip3B family insecticidal protein reveals a new fold and a unique tetrameric assembly. Protein Sci, 29, 824-829. PubMed id: 31840313 DOI: 10.1002/pro.3803

Date:

21-Nov-19 Release date: 18-Dec-19

Protein chains

A0A290WPI2  (A0A290WPI2_BACTU) -  Vegetative insecticidal protein from Bacillus thuringiensis

Seq: 803 a.a.

Struc: 752 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/pro.3803

Protein Sci 29:824-829 (2020)

PubMed id: 31840313

Crystal structure of a Vip3B family insecticidal protein reveals a new fold and a unique tetrameric assembly.

M.Zheng, A.G.Evdokimov, F.Moshiri, C.Lowder, J.Haas.

ABSTRACT

Vegetatively expressed insecticidal proteins (VIPs) produced by Bacillus thuringiensis fall into several classes of which the third, VIP3, is known for their activity against several key Lepidopteran pests of commercial broad acre crops and because their mode of action does not overlap with that of crystalline insecticidal proteins. The details of the VIP3 structure and mode of action have remained obscure for the quarter century that has passed since their discovery. In the present article, we report the first crystal structure of a full-length VIP3 protein. Crystallization of this target required multiple rounds of construct optimization and screening-over 200 individual sequences were expressed and tested. This protein adopts a novel global fold that combines domains with hitherto unreported topology and containing elements seemingly borrowed from carbohydrate-binding domains, lectins, or from other insecticidal proteins.