› 3tqt

X-ray diffraction
1.88Å resolution

Structure of the D-alanine-D-alanine ligase from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tqt/pdb
PDB entry 3tqt coloured by chain, front view.
PDB entry 3tqt coloured by chain, side view.
PDB entry 3tqt coloured by chain, top view.
Source organism: Coxiella burnetii RSA 493
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

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-182917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 372 amino acids
Theoretical weight: 41.27 KDa
Source organism: Coxiella burnetii RSA 493
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83BZ9 (Residues: 1-372; Coverage: 100%)
Gene names: CBU_1338, ddl
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 68.238Å b: 97.442Å c: 106.563Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.224
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more

1 mention without citation

Burkholderia pseudomallei d-alanine-d-alanine ligase; detailed characterisation and assessment of a potential antibiotic drug target.
Díaz-Sáez et al. (2019)