2KJ3

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

2KJ3 の概要

• エントリーDOI: 10.2210/pdb2kj3/pdb
• 関連するPDBエントリー: 2RNM
• 分子名称: Small s protein (1 entity in total)
• 機能のキーワード: het-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, protein fibril
• 由来する生物種: Podospora anserina
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26002.95

構造登録者

Van Melckebeke, H.,Wasmer, C.,Lange, A.,AB, E.,Loquet, A.,Meier, B.H. (登録日: 2009-05-20, 公開日: 2010-06-02, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

SOLID-STATE NMR