› 5ulv

X-ray diffraction
1.66Å resolution

Malate dehydrogenase from Methylobacterium extorquens

Released:
DOI: 10.2210/pdb5ulv/pdb
PDB entry 5ulv coloured by chain, front view.
PDB entry 5ulv coloured by chain, side view.
PDB entry 5ulv coloured by chain, top view.
Source organism: Methylorubrum extorquens
Primary publication:
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.
González JM, Marti-Arbona R, Chen JCH, Broom-Peltz B, Unkefer CJ
Acta Crystallogr F Struct Biol Commun 74 610-616 (2018)
PMID: 30279311

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 33.68 KDa
Source organism: Methylorubrum extorquens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q84FY8 (Residues: 1-320; Coverage: 100%)
Gene names: MexAM1_META1p1537, mdh
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6422
Unit cell:
a: 108.995Å b: 108.995Å c: 104.659Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.141 0.14 0.168
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

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)

1 mention without citation

Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.
González et al. (2018)