› 2wsb

X-ray diffraction
1.25Å resolution

Crystal structure of the short-chain dehydrogenase Galactitol- Dehydrogenase (GatDH) of Rhodobacter sphaeroides in complex with NAD

Released:
DOI: 10.2210/pdb2wsb/pdb
PDB entry 2wsb coloured by chain, front view.
PDB entry 2wsb coloured by chain, side view.
PDB entry 2wsb coloured by chain, top view.
Source organism: Cereibacter sphaeroides
Primary publication:
Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D.
Carius Y, Christian H, Faust A, Zander U, Klink BU, Kornberger P, Kohring GW, Giffhorn F, Scheidig AJ
J Biol Chem 285 20006-14 (2010)
PMID: 20410293

Function and Biology Details

Reaction catalysed: 
Galactitol + NAD(+) = L-tagatose + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110997 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactitol 2-dehydrogenase (L-tagatose-forming) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 254 amino acids
Theoretical weight: 26.41 KDa
Source organism: Cereibacter sphaeroides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C0KTJ6 (Residues: 1-254; Coverage: 100%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
2 bound ligands:
Ligand MG 2 x MG
Ligand POL 8 x POL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 97.79Å b: 106.62Å c: 109.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.134 0.177
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 citation in other articles

A short-chain dehydrogenase involved in terpene metabolism from Zingiber zerumbet.
Okamoto et al. (2011)
8 more

2 mentions without citation

Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme.
Dhindwal et al. (2011)
1 more