› 6u7l

X-ray diffraction
2.75Å resolution

2.75 Angstrom Crystal Structure of Galactarate Dehydratase from Escherichia coli.

Released:
DOI: 10.2210/pdb6u7l/pdb
PDB entry 6u7l coloured by chain, front view.
PDB entry 6u7l coloured by chain, side view.
PDB entry 6u7l coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of galactarate dehydratase, a new fold in an enolase involved in bacterial fitness after antibiotic treatment.
Rosas-Lemus M, Minasov G, Shuvalova L, Wawrzak Z, Kiryukhina O, Mih N, Jaroszewski L, Palsson B, Godzik A, Satchell KJF
Protein Sci 29 711-722 (2020)
PMID: 31811683

Function and Biology Details

Reaction catalysed: 
Galactarate = (2R,3S)-2,3-dihydroxy-5-oxohexanedioate + H(2)O
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-153961 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Galactarate dehydratase (L-threo-forming) Chains: A, B
Molecule details ›
Chains: A, B
Length: 526 amino acids
Theoretical weight: 57.33 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39829 (Residues: 1-523; Coverage: 100%)
Gene names: JW3097, b3128, garD, yhaG
Sequence domains:
Galactarate dehydratase (L-threo-forming) Chains: C, D
Molecule details ›
Chains: C, D
Length: 526 amino acids
Theoretical weight: 57.25 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39829 (Residues: 1-523; Coverage: 100%)
Gene names: JW3097, b3128, garD, yhaG
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CA 9 x CA
Ligand CL 7 x CL
2 modified residues:
Ligand MSE 44 x MSE
Ligand PHD 2 x PHD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 58.462Å b: 167.574Å c: 117.065Å
α: 90° β: 103.97° γ: 90°
R-values:
R R work R free
0.208 0.206 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Evolutionarily stable gene clusters shed light on the common grounds of pathogenicity in the Acinetobacter calcoaceticus-baumannii complex.
Djahanschiri et al. (2022)

1 mention without citation

Structure of galactarate dehydratase, a new fold in an enolase involved in bacterial fitness after antibiotic treatment.
Rosas-Lemus et al. (2020)