› 5d8d

X-ray diffraction
2.19Å resolution

Crystal structure of D-alanine-D-alanine ligase from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb5d8d/pdb
PDB entry 5d8d coloured by chain, front view.
PDB entry 5d8d coloured by chain, side view.
PDB entry 5d8d coloured by chain, top view.
Source organism: Acinetobacter baumannii ACICU
Primary publication:
The crystal structure of the D-alanine-D-alanine ligase from Acinetobacter baumannii suggests a flexible conformational change in the central domain before nucleotide binding.
Huynh KH, Hong MK, Lee C, Tran HT, Lee SH, Ahn YJ, Cha SS, Kang LW
J Microbiol 53 776-82 (2015)
PMID: 26502962

Function and Biology Details

Reaction catalysed: 
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanine ligase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 308 amino acids
Theoretical weight: 33.39 KDa
Source organism: Acinetobacter baumannii ACICU
Expression system: Escherichia coli
UniProt:
  • Canonical: B2I1J3 (Residues: 1-308; Coverage: 100%)
Gene names: ACICU_03532, ddl
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2
Unit cell:
a: 221.618Å b: 74.766Å c: 143.117Å
α: 90° β: 103.27° γ: 90°
R-values:
R R work R free
0.224 0.221 0.281
Expression system: Escherichia coli

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Citations

1 citations in other articles

Genome-Scale Metabolic Modeling Reveals Metabolic Alterations of Multidrug-Resistant Acinetobacter baumannii in a Murine Bloodstream Infection Model.
Zhao et al. (2020)