› 2wvo

X-ray diffraction
2.3Å resolution

Structure of the HET-S N-terminal domain

Released:
DOI: 10.2210/pdb2wvo/pdb
PDB entry 2wvo coloured by chain, front view.
PDB entry 2wvo coloured by chain, side view.
PDB entry 2wvo coloured by chain, top view.
Source organism: Podospora anserina
Primary publication:
The mechanism of prion inhibition by HET-S.
Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R
Mol Cell 38 889-99 (2010)
PMID: 20620958

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heterokaryon incompatibility protein S Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.16 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B2ACC7 (Residues: 1-227; Coverage: 79%)
Gene names: PODANS_3_620, Pa_3_620, big S, het-S
Sequence domains: Prion-inhibition and propagation
Structure domains: Prion-inhibition and propagation, HeLo domain

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 95.26Å b: 95.26Å c: 170.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.225 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Biology and genetics of prions causing neurodegeneration.
Prusiner SB. (2013)
16 more

3 mentions without citation

The HET-S/s Prion Motif in the Control of Programmed Cell Death.
Riek et al. (2016)
2 more