3jsl

X-ray diffraction
1.8Å resolution

Crystal structure of the adenylation domain of NAD+-dependent DNA ligase from Staphylococcus aureus

Released:
Source organism: Staphylococcus aureus
Primary publication:
Structure of the adenylation domain of NAD(+)-dependent DNA ligase from Staphylococcus aureus.
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 1078-82 (2009)
PMID: 19923722

Function and Biology Details

Reaction catalysed:
(1a) NAD(+) + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + beta-nicotinamide D-nucleotide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 36.72 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AIU7 (Residues: 1-312; Coverage: 47%)
Gene names: lig, ligA
Sequence domains: NAD-dependent DNA ligase adenylation domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 40.152Å b: 49.193Å c: 88.039Å
α: 90.1° β: 103.2° γ: 90.01°
R-values:
R R work R free
0.198 0.196 0.25
Expression system: Escherichia coli