› 1uxk

X-ray diffraction
1.8Å 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/pdb1uxk/pdb
PDB entry 1uxk coloured by chain, front view.
PDB entry 1uxk coloured by chain, side view.
PDB entry 1uxk 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, C
Molecule details ›
Chains: A, C
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
3 bound ligands:
Ligand CD 10 x CD
Ligand CL 2 x CL
Ligand NA 6 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P3121
Unit cell:
a: 105.405Å b: 105.405Å c: 102.305Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.214
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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