› 1gv0

X-ray diffraction
2.5Å resolution

Structural Basis for Thermophilic Protein Stability: Structures of Thermophilic and Mesophilic Malate Dehydrogenases

Released:
DOI: 10.2210/pdb1gv0/pdb
PDB entry 1gv0 coloured by chain, front view.
PDB entry 1gv0 coloured by chain, side view.
PDB entry 1gv0 coloured by chain, top view.
Source organism: Chlorobaculum tepidum
Primary publication:
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases.
Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjørk A, Synstad B, Naterstad K, Sirevåg R, Eklund H
J Mol Biol 318 707-21 (2002)
PMID: 12054817

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 33.14 KDa
Source organism: Chlorobaculum tepidum
Expression system: Escherichia coli
UniProt:
  • Canonical: P80039 (Residues: 1-310; Coverage: 100%)
Gene names: CT1507, mdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: C2221
Unit cell:
a: 114.32Å b: 149.42Å c: 97.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.275
Expression system: Escherichia coli

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Citations

4 review citations

Rational engineering of enzyme stability.
Eijsink et al. (2004)
3 more