› 1gv1

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb1gv1/pdb
PDB entry 1gv1 coloured by chain, front view.
PDB entry 1gv1 coloured by chain, side view.
PDB entry 1gv1 coloured by chain, top view.
Source organism: Prosthecochloris vibrioformis
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-143170 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 33.31 KDa
Source organism: Prosthecochloris vibrioformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C890 (Residues: 1-310; Coverage: 100%)
Gene name: mdh
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 64.425Å b: 85.824Å c: 117.498Å
α: 90° β: 104.61° γ: 90°
R-values:
R R work R free
0.216 0.216 0.305
Expression system: Escherichia coli

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Citations

4 review citations

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

4 mentions without citation

Molecular signature of hypersaline adaptation: insights from genome and proteome composition of halophilic prokaryotes.
Paul et al. (2008)
3 more