› 2wvn

X-ray diffraction
2.62Å resolution

Structure of the HET-s N-terminal domain

Released:
DOI: 10.2210/pdb2wvn/pdb
PDB entry 2wvn coloured by chain, front view.
PDB entry 2wvn coloured by chain, side view.
PDB entry 2wvn 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-169926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heterokaryon incompatibility protein s Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.53 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03689 (Residues: 1-227; Coverage: 79%)
Gene names: het-s, small s
Sequence domains: Prion-inhibition and propagation
Structure domains: Prion-inhibition and propagation, HeLo domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P432
Unit cell:
a: 122.66Å b: 122.66Å c: 122.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.216 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

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

2 mentions without citation

The mechanism of prion inhibition by HET-S.
Greenwald et al. (2010)
1 more