2KJ3

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

Summary for 2KJ3

• Entry DOI: 10.2210/pdb2kj3/pdb
• Related: 2RNM
• Descriptor: Small s protein (1 entity in total)
• Functional Keywords: het-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, protein fibril
• Biological source: Podospora anserina
• Total number of polymer chains: 3
• Total formula weight: 26002.95

Authors

Van Melckebeke, H.,Wasmer, C.,Lange, A.,AB, E.,Loquet, A.,Meier, B.H. (deposition date: 2009-05-20, release date: 2010-06-02, Last modification date: 2024-05-01)

Primary citation

Van Melckebeke, H.,Wasmer, C.,Lange, A.,AB, E.,Loquet, A.,Bockmann, A.,Meier, B.H.
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
J.Am.Chem.Soc., 132:13765-13775, 2010

PubMed Abstract: 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.

PubMed: 20828131
DOI: 10.1021/ja104213j

Experimental method

SOLID-STATE NMR