› 1u6z

X-ray diffraction
1.9Å resolution

Structure of an E. coli Exopolyphosphatase: Insight into the processive hydrolysis of polyphosphate and its regulation

Released:
DOI: 10.2210/pdb1u6z/pdb
PDB entry 1u6z coloured by chain, front view.
PDB entry 1u6z coloured by chain, side view.
PDB entry 1u6z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Origin of exopolyphosphatase processivity: Fusion of an ASKHA phosphotransferase and a cyclic nucleotide phosphodiesterase homolog.
Alvarado J, Ghosh A, Janovitz T, Jauregui A, Hasson MS, Sanders DA
Structure 14 1263-72 (2006)
PMID: 16905100

Function and Biology Details

Reaction catalysed: 
(Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exopolyphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 513 amino acids
Theoretical weight: 58.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AFL6 (Residues: 1-513; Coverage: 100%)
Gene names: JW2487, b2502, ppx
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 29 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P41212
Unit cell:
a: 89.144Å b: 89.144Å c: 350.686Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.204 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Inorganic polyphosphate: essential for growth and survival.
Rao et al. (2009)
5 more

7 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
6 more