› 2x0i

X-ray diffraction
2.91Å resolution

2.9 A RESOLUTION STRUCTURE OF MALATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS IN COMPLEX WITH NADH

Released:
DOI: 10.2210/pdb2x0i/pdb
PDB entry 2x0i coloured by chain, front view.
PDB entry 2x0i coloured by chain, side view.
PDB entry 2x0i coloured by chain, top view.
Source organism: Archaeoglobus fulgidus DSM 4304
Primary publication:
The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation.
Irimia A, Vellieux FM, Madern D, Zaccaï G, Karshikoff A, Tibbelin G, Ladenstein R, Lien T, Birkeland NK
J Mol Biol 335 343-56 (2004)
PMID: 14659762

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126615 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 31.91 KDa
Source organism: Archaeoglobus fulgidus DSM 4304
Expression system: Escherichia coli
UniProt:
  • Canonical: O08349 (Residues: 1-294; Coverage: 100%)
Gene names: AF_0855, mdh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 1 x NAI
2 bound ligands:
Ligand SO4 1 x SO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41212
Unit cell:
a: 112.964Å b: 112.964Å c: 71.294Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.152 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Adaptation to high temperatures through macromolecular dynamics by neutron scattering.
Tehei et al. (2007)
15 other articles

1 mention without citation

Protein Conformational Space at the Edge of Allostery: Turning a Nonallosteric Malate Dehydrogenase into an "Allosterized" Enzyme Using Evolution-Guided Punctual Mutations.
Iorio et al. (2022)