3kwv

X-ray diffraction
3.1Å resolution

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

Released:

Function and Biology Details

Reaction catalysed:
Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-146589 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protective antigen PA-63 Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 548 amino acids
Theoretical weight: 61.48 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13423 (Residues: 197-764; Coverage: 75%)
Gene names: BXA0164, GBAA_pXO1_0164, pXO1-110, pag, pagA
Sequence domains:
Structure domains:
Lethal factor Chains: C, F
Molecule details ›
Chains: C, F
Length: 263 amino acids
Theoretical weight: 30.55 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15917 (Residues: 34-296; Coverage: 34%)
Gene names: BXA0172, GBAA_pXO1_0172, lef, pXO1-107
Sequence domains: Anthrax toxin lethal factor, N- and C-terminal domain
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P4212
Unit cell:
a: 178.381Å b: 178.381Å c: 240.363Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.249 0.281
Expression system: Escherichia coli BL21(DE3)