› 6sk1

X-ray diffraction
1.5Å resolution

Diaminobutyrate acetyltransferase EctA from Paenibacillus lautus in complex with coenzyme A

Released:
DOI: 10.2210/pdb6sk1/pdb
PDB entry 6sk1 coloured by chain, front view.
PDB entry 6sk1 coloured by chain, side view.
PDB entry 6sk1 coloured by chain, top view.
Source organism: Paenibacillus sp. Y412MC10
Primary publication:
The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.
Richter AA, Kobus S, Czech L, Hoeppner A, Zarzycki J, Erb TJ, Lauterbach L, Dickschat JS, Bremer E, Smits SHJ
J Biol Chem 295 2822-2838 (2020)
PMID: 31969391

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-2,4-diaminobutanoate = CoA + N(4)-acetyl-L-2,4-diaminobutanoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112472 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-2,4-diaminobutyric acid acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 20.83 KDa
Source organism: Paenibacillus sp. Y412MC10
Expression system: Escherichia coli
UniProt:
  • Canonical: D3EKC1 (Residues: 1-170; Coverage: 100%)
Gene names: GYMC10_5665, ectA
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments


Cofactor: Ligand COA 1 x COA
1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43212
Unit cell:
a: 68.282Å b: 68.282Å c: 79.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.183
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.
Mais et al. (2020)
5 more

2 mentions without citation

The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.
Richter et al. (2020)
1 more