› 2ixp

X-ray diffraction
2.8Å resolution

Crystal structure of the Pp2A phosphatase activator Ypa1 PTPA1 in complex with model substrate

Released:
DOI: 10.2210/pdb2ixp/pdb
PDB entry 2ixp coloured by chain, front view.
PDB entry 2ixp coloured by chain, side view.
PDB entry 2ixp coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity.
Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, van Tilbeurgh H, Goris J
Mol Cell 23 413-24 (2006)
PMID: 16885030

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154116 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2A activator 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 323 amino acids
Theoretical weight: 37.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40454 (Residues: 1-317; Coverage: 81%)
Gene names: NCS1, RRD1, YIL153W, YPA1
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
SIN-ALA-ALA-PRO-LYS-NIT Chains: F, G, H, I
Molecule details ›
Chains: F, G, H, I
Length: 6 amino acids
Theoretical weight: 607 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P65
Unit cell:
a: 86.886Å b: 86.886Å c: 410.626Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.229 0.302
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

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

2 mentions without citation

Evolution of domain-peptide interactions to coadapt specificity and affinity to functional diversity.
Kelil et al. (2016)
1 more