› 3wgb

X-ray diffraction
2.6Å resolution

Crystal structure of aeromonas jandaei L-allo-threonine aldolase

Released:
DOI: 10.2210/pdb3wgb/pdb
PDB entry 3wgb coloured by chain, front view.
PDB entry 3wgb coloured by chain, side view.
PDB entry 3wgb coloured by chain, top view.
Source organism: Aeromonas jandaei
Primary publication:
L-allo-threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.
Qin HM, Imai FL, Miyakawa T, Kataoka M, Kitamura N, Urano N, Mori K, Kawabata H, Okai M, Ohtsuka J, Hou F, Nagata K, Shimizu S, Tanokura M
Acta Crystallogr D Biol Crystallogr 70 1695-703 (2014)
PMID: 24914980

Function and Biology Details

Reaction catalysed: 
L-allo-threonine = glycine + acetaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126559 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-allo-threonine aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 36.61 KDa
Source organism: Aeromonas jandaei
Expression system: Escherichia coli
UniProt:
  • Canonical: O07051 (Residues: 1-338; Coverage: 100%)
Gene name: ltaA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PLG 4 x PLG
Ligand GLY 1 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 82.474Å b: 95.85Å c: 94.884Å
α: 90° β: 113.64° γ: 90°
R-values:
R R work R free
0.235 0.233 0.283
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
1 more

4 mentions without citation

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.
Fesko K. (2016)
3 more