› 1guy

X-ray diffraction
2.2Å resolution

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

Released:
DOI: 10.2210/pdb1guy/pdb
PDB entry 1guy coloured by chain, front view.
PDB entry 1guy coloured by chain, side view.
PDB entry 1guy coloured by chain, top view.
Source organism: Chloroflexus aurantiacus
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:
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
1 bound ligand:
Ligand CD 5 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P3121
Unit cell:
a: 106.67Å b: 106.67Å c: 103.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.197
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

An experimental point of view on hydration/solvation in halophilic proteins.
Talon et al. (2014)