› 2j82

X-ray diffraction
1.28Å resolution

Structural analysis of the PP2C Family Phosphatase tPphA from Thermosynechococcus elongatus

Released:
DOI: 10.2210/pdb2j82/pdb
PDB entry 2j82 coloured by chain, front view.
PDB entry 2j82 coloured by chain, side view.
PDB entry 2j82 coloured by chain, top view.
Source organism: Synechococcus elongatus
Primary publication:
Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site.
Schlicker C, Fokina O, Kloft N, Grüne T, Becker S, Sheldrick GM, Forchhammer K
J Mol Biol 376 570-81 (2008)
PMID: 18164312

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein-serine/threonine phosphatase Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 26.74 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8DGS1 (Residues: 1-240; Coverage: 100%)
Gene name: tlr2243
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2221
Unit cell:
a: 38.216Å b: 151.799Å c: 82.505Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 not available 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
9 more

6 mentions without citation

A third metal is required for catalytic activity of the signal-transducing protein phosphatase M tPphA.
Su et al. (2011)
5 more