› 3hqq

X-ray diffraction
5.07Å resolution

Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with Fructose 2,6 bisphosphate

Released:
DOI: 10.2210/pdb3hqq/pdb
PDB entry 3hqq coloured by chain, front view.
PDB entry 3hqq coloured by chain, side view.
PDB entry 3hqq coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model.
Morgan HP, McNae IW, Nowicki MW, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD
J Biol Chem 285 12892-8 (2010)
PMID: 20123988

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 499 amino acids
Theoretical weight: 54.47 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27686 (Residues: 1-499; Coverage: 100%)
Gene name: PYK
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand FDP 24 x FDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 243.84Å b: 254.69Å c: 892.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.353 0.353 0.357
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Metalloproteins in the Biology of Heterocysts.
Pernil et al. (2019)
1 more

5 mentions without citation

An overview of structure, function, and regulation of pyruvate kinases.
Schormann et al. (2019)
4 more