› 2zqz

X-ray diffraction
2.5Å resolution

R-state structure of allosteric L-lactate dehydrogenase from Lactobacillus casei

Released:
DOI: 10.2210/pdb2zqz/pdb
PDB entry 2zqz coloured by chain, front view.
PDB entry 2zqz coloured by chain, side view.
PDB entry 2zqz coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase.
Arai K, Ishimitsu T, Fushinobu S, Uchikoba H, Matsuzawa H, Taguchi H
Proteins 78 681-94 (2010)
PMID: 19787773

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 326 amino acids
Theoretical weight: 35.57 KDa
Source organism: Lacticaseibacillus casei
Expression system: Escherichia coli
UniProt:
  • Canonical: P00343 (Residues: 1-326; Coverage: 100%)
Gene name: ldh
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 164.382Å b: 82.893Å c: 179.771Å
α: 90° β: 91.21° γ: 90°
R-values:
R R work R free
0.212 0.212 0.271
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions.
Colletier et al. (2012)
10 more

1 mention without citation

The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
Ikehara et al. (2014)