1YJP

Structure of GNNQQNY from yeast prion Sup35

1YJP の概要

• エントリーDOI: 10.2210/pdb1yjp/pdb
• 関連するPDBエントリー: 1YJO
• 分子名称: Eukaryotic peptide chain release factor GTP-binding subunit (2 entities in total)
• 機能のキーワード: beta sheet, steric zipper, glutamine zipper, asparagine zipper, protein binding
• 細胞内の位置: Cytoplasm : P05453
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 836.81

構造登録者

Nelson, R.,Sawaya, M.R.,Balbirnie, M.,Madsen, A.O.,Riekel, C.,Grothe, R.,Eisenberg, D. (登録日: 2005-01-15, 公開日: 2005-06-14, 最終更新日: 2024-02-14)

主引用文献

Nelson, R.,Sawaya, M.R.,Balbirnie, M.,Madsen, A.O.,Riekel, C.,Grothe, R.,Eisenberg, D.
Structure of the cross-beta spine of amyloid-like fibrils.
Nature, 435:773-778, 2005

PubMed Abstract: Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.

PubMed: 15944695
DOI: 10.1038/nature03680

実験手法

X-RAY DIFFRACTION (1.8 Å)