› 1o6z

X-ray diffraction
1.95Å resolution

1.95 A resolution structure of (R207S,R292S) mutant of malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (holo form)

Released:
DOI: 10.2210/pdb1o6z/pdb
PDB entry 1o6z coloured by chain, front view.
PDB entry 1o6z coloured by chain, side view.
PDB entry 1o6z coloured by chain, top view.
Source organism: Haloarcula marismortui
Primary publication:
The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies.
Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FM
J Mol Biol 326 859-73 (2003)
PMID: 12581646

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-170550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 303 amino acids
Theoretical weight: 32.57 KDa
Source organism: Haloarcula marismortui
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07841 (Residues: 2-304; Coverage: 100%)
Gene names: mdh, rrnAC2706
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand CL 8 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 126.64Å b: 114.42Å c: 124.87Å
α: 90° β: 93.11° γ: 90°
R-values:
R R work R free
0.194 0.19 0.263
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Halophiles and their enzymes: negativity put to good use.
DasSarma et al. (2015)
3 more