› 1kzh

X-ray diffraction
2.55Å resolution

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

Released:
DOI: 10.2210/pdb1kzh/pdb
PDB entry 1kzh coloured by chain, front view.
PDB entry 1kzh coloured by chain, side view.
PDB entry 1kzh coloured by chain, top view.
Source organism: Borreliella burgdorferi
Primary publication:
The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
Moore SA, Ronimus RS, Roberson RS, Morgan HW
Structure 10 659-71 (2002)
PMID: 12015149

Function and Biology Details

Reaction catalysed: 
Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 555 amino acids
Theoretical weight: 62.55 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli
UniProt:
  • Canonical: P70826 (Residues: 1-555; Coverage: 100%)
Gene names: BB_0020, PFK2, pfp, pfpB
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 85.098Å b: 97.926Å c: 148.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.243
Expression system: Escherichia coli

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Citations

2 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
1 more

2 mentions without citation

Suppression of Drug Resistance Reveals a Genetic Mechanism of Metabolic Plasticity in Malaria Parasites.
Guggisberg et al. (2018)
1 more