› 2bl4

X-ray diffraction
2.85Å resolution

Lactaldehyde:1,2-propanediol oxidoreductase of Escherichia coli

Released:
DOI: 10.2210/pdb2bl4/pdb
PDB entry 2bl4 coloured by chain, front view.
PDB entry 2bl4 coloured by chain, side view.
PDB entry 2bl4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
Montella C, Bellsolell L, Pérez-Luque R, Badía J, Baldoma L, Coll M, Aguilar J
J Bacteriol 187 4957-66 (2005)
PMID: 15995211

Function and Biology Details

Reaction catalysed: 
(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141921 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactaldehyde reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 41.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9S1 (Residues: 1-382; Coverage: 100%)
Gene names: JW2770, b2799, fucO
Sequence domains: Iron-containing alcohol dehydrogenase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand FE2 2 x FE2
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P3121
Unit cell:
a: 109.422Å b: 109.422Å c: 182.459Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.251 0.303
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Biosynthesis of phosphonic and phosphinic acid natural products.
Metcalf et al. (2009)
2 more

9 mentions without citation

Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners.
Haft DH. (2011)
8 more