5I55

Crystal Structure of the Virulent PSM-alpha3 Peptide Forming a Cross-alpha amyloid-like Fibril

5I55 の概要

• エントリーDOI: 10.2210/pdb5i55/pdb
• 分子名称: Psm alpha-3, (4S)-2-METHYL-2,4-PENTANEDIOL, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: the cross-alpha amyloid-like fold is composed of mating alpha-helical sheets, protein fibril
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2835.26

構造登録者

Landau, M.,Moshe, A.,Tayeb-Fligelman, E.,Sawaya, M.R.,Coquelle, N.,Colletier, J.-P. (登録日: 2016-02-14, 公開日: 2017-03-01, 最終更新日: 2024-10-09)

主引用文献

Tayeb-Fligelman, E.,Tabachnikov, O.,Moshe, A.,Goldshmidt-Tran, O.,Sawaya, M.R.,Coquelle, N.,Colletier, J.P.,Landau, M.
The cytotoxic Staphylococcus aureus PSM alpha 3 reveals a cross-alpha amyloid-like fibril.
Science, 355:831-833, 2017

PubMed Abstract: Amyloids are ordered protein aggregates, found in all kingdoms of life, and are involved in aggregation diseases as well as in physiological activities. In microbes, functional amyloids are often key virulence determinants, yet the structural basis for their activity remains elusive. We determined the fibril structure and function of the highly toxic, 22-residue phenol-soluble modulin α3 (PSMα3) peptide secreted by PSMα3 formed elongated fibrils that shared the morphological and tinctorial characteristics of canonical cross-β eukaryotic amyloids. However, the crystal structure of full-length PSMα3, solved de novo at 1.45 angstrom resolution, revealed a distinctive "cross-α" amyloid-like architecture, in which amphipathic α helices stacked perpendicular to the fibril axis into tight self-associating sheets. The cross-α fibrillation of PSMα3 facilitated cytotoxicity, suggesting that this assembly mode underlies function in .

PubMed: 28232575
DOI: 10.1126/science.aaf4901

実験手法

X-RAY DIFFRACTION (1.45 Å)