› 2rnm

Solution NMR

Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Released:
DOI: 10.2210/pdb2rnm/pdb
PDB entry 2rnm coloured by chain, ensemble of 20 models, front view.
PDB entry 2rnm coloured by chain, ensemble of 20 models, side view.
PDB entry 2rnm coloured by chain, ensemble of 20 models, top view.
Source organism: Podospora anserina
Primary publication:
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.
Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH
Science 319 1523-6 (2008)
PMID: 18339938

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heterokaryon incompatibility protein s Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 79 amino acids
Theoretical weight: 8.67 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03689 (Residues: 217-289; Coverage: 25%)
Gene names: het-s, small s
Sequence domains: Het-s 218-289

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

137 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
136 more

30 mentions without citation

Solid-state NMR studies of amyloid fibril structure.
Tycko R. (2011)
29 more