› 3e0v

X-ray diffraction
3.3Å resolution

Crystal structure of pyruvate kinase from Leishmania mexicana in complex with sulphate ions

Released:
DOI: 10.2210/pdb3e0v/pdb
PDB entry 3e0v coloured by chain, front view.
PDB entry 3e0v coloured by chain, side view.
PDB entry 3e0v coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Sulphate removal induces a major conformational change in Leishmania mexicana pyruvate kinase in the crystalline state.
Tulloch LB, Morgan HP, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD
J Mol Biol 383 615-26 (2008)
PMID: 18775437

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
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-173276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 539 amino acids
Theoretical weight: 58.87 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27686 (Residues: 1-499; Coverage: 100%)
Gene name: PYK
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 40 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P42212
Unit cell:
a: 261.955Å b: 261.955Å c: 185.541Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.29
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Methicillin-resistant Staphylococcus aureus (MRSA) pyruvate kinase as a target for bis-indole alkaloids with antibacterial activities.
Zoraghi et al. (2011)
9 more

2 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
1 more