› 1uxg

X-ray diffraction
1.9Å resolution

Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.

Released:
DOI: 10.2210/pdb1uxg/pdb
PDB entry 1uxg coloured by chain, front view.
PDB entry 1uxg coloured by chain, side view.
PDB entry 1uxg coloured by chain, top view.
Source organism: Chloroflexus aurantiacus
Primary publication:
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.
Bjørk A, Dalhus B, Mantzilas D, Sirevåg R, Eijsink VG
J Mol Biol 341 1215-26 (2004)
PMID: 15321717

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160336 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.75 KDa
Source organism: Chloroflexus aurantiacus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80040 (Residues: 1-309; Coverage: 100%)
Gene names: Caur_0900, mdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand FUM 2 x FUM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P43212
Unit cell:
a: 149.832Å b: 149.832Å c: 110.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.27
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Directed evolution of enzyme stability.
Eijsink et al. (2005)
1 more