› 3umo

X-ray diffraction
1.7Å resolution

Crystal structure of the Phosphofructokinase-2 from Escherichia coli in complex with Potassium

Released:
DOI: 10.2210/pdb3umo/pdb
PDB entry 3umo coloured by chain, front view.
PDB entry 3umo coloured by chain, side view.
PDB entry 3umo coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
A ribokinase family conserved monovalent cation binding site enhances the MgATP-induced inhibition in E. coli phosphofructokinase-2.
Baez M, Cabrera R, Pereira HM, Blanco A, Villalobos P, Ramírez-Sarmiento CA, Caniuguir A, Guixé V, Garratt RC, Babul J
Biophys J 105 185-93 (2013)
PMID: 23823238

Function and Biology Details

Reaction catalysed: 
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase isozyme 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.49 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06999 (Residues: 1-309; Coverage: 100%)
Gene names: JW5280, b1723, pfkB
Sequence domains: pfkB family carbohydrate kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand ATP 4 x ATP
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P2221
Unit cell:
a: 43.812Å b: 88.77Å c: 176.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.208
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Role of monovalent and divalent metal cations in human ribokinase catalysis and regulation.
Quiroga-Roger et al. (2015)
4 more

2 mentions without citation

The phosphocarrier protein HPr of the bacterial phosphotransferase system globally regulates energy metabolism by directly interacting with multiple enzymes in Escherichia coli.
Rodionova et al. (2017)
1 more