› 2wvq

X-ray diffraction
2Å resolution

Structure of the HET-s N-terminal domain. Mutant D23A, P33H

Released:
DOI: 10.2210/pdb2wvq/pdb
PDB entry 2wvq coloured by chain, front view.
PDB entry 2wvq coloured by chain, side view.
PDB entry 2wvq 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.46 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03689 (Residues: 13-221; Coverage: 72%)
Gene names: het-s, small s
Sequence domains: Prion-inhibition and propagation
Structure domains: Prion-inhibition and propagation, HeLo domain

Ligands and Environments

2 bound ligands:
Ligand DTT 1 x DTT
Ligand DTU 1 x DTU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 49.33Å b: 83.15Å c: 67.36Å
α: 90° β: 104.55° γ: 90°
R-values:
R R work R free
0.227 0.225 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

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

1 mention without citation

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