› 4pzp

X-ray diffraction
1.9Å resolution

Substrate-free structure of D-alanine carrier protein ligase DltA from Bacillus cereus

Released:
DOI: 10.2210/pdb4pzp/pdb
PDB entry 4pzp coloured by chain, front view.
PDB entry 4pzp coloured by chain, side view.
PDB entry 4pzp coloured by chain, top view.
Source organism: Bacillus cereus ATCC 14579
Primary publication:
Thiolation-enhanced substrate recognition by D-alanyl carrier protein ligase DltA from Bacillus cereus.
Du L, Luo Y
F1000Res 3 106 (2014)
PMID: 25285205

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-182523 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanyl carrier protein ligase Chain: A
Molecule details ›
Chain: A
Length: 512 amino acids
Theoretical weight: 57.57 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q81G39 (Residues: 2-504; Coverage: 100%)
Gene names: BC_1372, dltA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 52.9Å b: 81.9Å c: 59.3Å
α: 90° β: 108.3° γ: 90°
R-values:
R R work R free
0.21 0.21 0.261
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Structural basis of the nonribosomal codes for nonproteinogenic amino acid selective adenylation enzymes in the biosynthesis of natural products.
Kudo et al. (2019)
4 other articles

3 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
2 more