4whn

X-ray diffraction
2.15Å resolution

Structure of toxin-activating acyltransferase (TAAT)

Released:
Primary publication:
Structure of a bacterial toxin-activating acyltransferase.
Proc Natl Acad Sci U S A 112 E3058-66 (2015)
PMID: 26016525

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RTX-I toxin-activating lysine-acyltransferase ApxIC Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 183 amino acids
Theoretical weight: 21.2 KDa
Source organism: Actinobacillus pleuropneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P55132 (Residues: 2-172; Coverage: 99%)
Gene names: apxC, apxIC, clyIC, hlyIC
Sequence domains: RTX toxin acyltransferase family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 82.45Å b: 86.37Å c: 131.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.242
Expression system: Escherichia coli