Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy

J Am Chem Soc. 2010 Oct 6;132(39):13765-75. doi: 10.1021/ja104213j.


We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s in its amyloid form. On the basis of 134 unambiguous distance restraints, we recently showed that HET-s(218-289) in its fibrillar state forms a left-handed β-solenoid, and an atomic-resolution NMR structure of the triangular core was determined from unambiguous restraints only. In this paper, we go considerably further and present a comprehensive protocol using six differently labeled samples, a collection of optimized solid-state NMR experiments, and adapted structure calculation protocols. The high-resolution structure obtained includes the less ordered but biologically important C-terminal part and improves the overall accuracy by including a large number of ambiguous distance restraints.

MeSH terms

  • Fungal Proteins / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation


  • Fungal Proteins
  • HET-S protein, Podospora anserina

Associated data

  • PDB/2KJ3