3bv8

X-ray diffraction
1.75Å resolution

Crystal structure of the N-terminal domain of tetrahydrodipicolinate acetyltransferase from Staphylococcus aureus

Released:
Entry authors: Cuff ME, Duggan E, Clancy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + L-2-acetamido-6-oxoheptanedioate
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
PDBe Complex ID:
PDB-CPX-181322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10.1 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7A2S0 (Residues: 5-88; Coverage: 35%)
Gene names: SAV1397, dapH
Sequence domains: Tetrahydrodipicolinate succinyltransferase N-terminal
Structure domains: Malonyl-CoA ACP transacylase, ACP-binding

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P6322
Unit cell:
a: 76.503Å b: 76.503Å c: 93.862Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.197
Expression system: Escherichia coli BL21(DE3)