› 2kj3

Solid-state NMR

High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Released:
DOI: 10.2210/pdb2kj3/pdb
PDB entry 2kj3 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kj3 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kj3 coloured by chain, ensemble of 20 models, top view.
Source organism: Podospora anserina
Primary publication:
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
J Am Chem Soc 132 13765-75 (2010)
PMID: 20828131

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heterokaryon incompatibility protein s Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 79 amino acids
Theoretical weight: 8.67 KDa
Source organism: Podospora anserina
Expression system: Escherichia coli BL21
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: simulated annealing, TORSION ANGLE DYNAMICS
Expression system: Escherichia coli BL21

Quick links

Citations

36 review citations

Prions in yeast.
Liebman et al. (2012)
35 more

29 mentions without citation

Molecular structures of amyloid and prion fibrils: consensus versus controversy.
Tycko et al. (2013)
28 more