› 1lth

X-ray diffraction
2.5Å resolution

T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

Released:
DOI: 10.2210/pdb1lth/pdb
PDB entry 1lth coloured by chain, front view.
PDB entry 1lth coloured by chain, side view.
PDB entry 1lth coloured by chain, top view.
Source organism: Bifidobacterium longum subsp. longum
Primary publication:
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T
Nat Struct Biol 1 176-85 (1994)
PMID: 7656036

Function and Biology Details

Reaction catalysed: 
(S)-lactate + NAD(+) = pyruvate + 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-123104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate dehydrogenase 2 Chains: R, T
Molecule details ›
Chains: R, T
Length: 319 amino acids
Theoretical weight: 34.13 KDa
Source organism: Bifidobacterium longum subsp. longum
Expression system: Escherichia coli
UniProt:
  • Canonical: E8ME30 (Residues: 2-320; Coverage: 100%)
Gene names: BLLJ_1290, ldh2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand FBP 2 x FBP
Ligand OXM 1 x OXM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: F222
Unit cell:
a: 148.4Å b: 295.9Å c: 71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structural symmetry and protein function.
Goodsell et al. (2000)
10 more

10 mentions without citation

Structure and evolution of the bifidobacterial carbohydrate metabolism proteins and enzymes.
Fushinobu et al. (2021)
9 more