6hvl

X-ray diffraction
2.8Å resolution

CdaA complex with c-di-AMP and AMP

Released:
Source organism: Listeria monocytogenes EGD-e
Primary publication:
Crystal structures of the c-di-AMP-synthesizing enzyme CdaA.
J Biol Chem 294 10463-10470 (2019)
PMID: 31118276

Function and Biology Details

Reaction catalysed:
2 ATP = 2 diphosphate + cyclic di-3',5'-adenylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-186956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diadenylate cyclase Chains: A, B
Molecule details ›
Chains: A, B
Length: 178 amino acids
Theoretical weight: 19.37 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Y5E4 (Residues: 101-273; Coverage: 63%)
Gene names: cdaA, dacA, lmo2120
Sequence domains: DisA bacterial checkpoint controller nucleotide-binding

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: R32
Unit cell:
a: 121.9Å b: 121.9Å c: 141.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.234
Expression system: Escherichia coli BL21(DE3)