› 3e7x

X-ray diffraction
2.6Å resolution

Crystal structure of DLTA: implications for the reaction mechanism of non-ribosomal peptide synthetase (NRPS) adenylation domains

Released:
DOI: 10.2210/pdb3e7x/pdb
PDB entry 3e7x coloured by chain, front view.
PDB entry 3e7x coloured by chain, side view.
PDB entry 3e7x coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains.
Yonus H, Neumann P, Zimmermann S, May JJ, Marahiel MA, Stubbs MT
J Biol Chem 283 32484-91 (2008)
PMID: 18784082

Function and Biology Details

Reaction catalysed: 
(1a) ATP + D-alanine = (D-alanyl)adenylate + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanyl carrier protein ligase Chain: A
Molecule details ›
Chain: A
Length: 511 amino acids
Theoretical weight: 56.94 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39581 (Residues: 1-503; Coverage: 100%)
Gene names: BSU38500, dae, dltA, ipa-5r
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AMP 1 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 45.765Å b: 91.389Å c: 121.471Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.238
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Lipoteichoic acid synthesis and function in gram-positive bacteria.
Percy et al. (2014)
17 more

3 mentions without citation

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
2 more