› 4pkm

X-ray diffraction
1.65Å resolution

Crystal Structure of Bacillus thuringiensis Cry51Aa1 Protoxin at 1.65 Angstroms Resolution

Released:
DOI: 10.2210/pdb4pkm/pdb
PDB entry 4pkm coloured by chain, front view.
PDB entry 4pkm coloured by chain, side view.
PDB entry 4pkm coloured by chain, top view.
Source organism: Bacillus thuringiensis F14-1
Primary publication:
Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type β-pore-forming toxin from Bacillus thuringiensis.
Xu C, Chinte U, Chen L, Yao Q, Meng Y, Zhou D, Bi LJ, Rose J, Adang MJ, Wang BC, Yu Z, Sun M
Biochem Biophys Res Commun 462 184-9 (2015)
PMID: 25957471

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108265 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Crystal protein Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 34.01 KDa
Source organism: Bacillus thuringiensis F14-1
Expression system: Bacillus thuringiensis BMB171
UniProt:
  • Canonical: A7IZR5 (Residues: 1-309; Coverage: 100%)
Gene name: cry51Aa1
Sequence domains: Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand SO4 1 x SO4
Ligand GLY 3 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P43212
Unit cell:
a: 54.703Å b: 54.703Å c: 209.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.199
Expression system: Bacillus thuringiensis BMB171

Quick links

Citations

2 review citations

Structural classification of insecticidal proteins - Towards an in silico characterisation of novel toxins.
Berry et al. (2017)
1 more

5 mentions without citation

The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins.
Dementiev et al. (2016)
4 more