7YAT

CryoEM tetra protofilament structure of the hamster prion 108-144 fibril

7YAT の概要

• エントリーDOI: 10.2210/pdb7yat/pdb
• EMDBエントリー: 33719
• 分子名称: Major prion protein (2 entities in total)
• 機能のキーワード: prion, fibril, hamster, protein fibril
• 由来する生物種: Mesocricetus auratus (golden hamster)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 59998.92

構造登録者

Chen, E.H.-L.,Kao, S.-W.,Lee, C.-H.,Huang, J.Y.C.,Chen, R.P.-Y.,Wu, K.-P. (登録日: 2022-06-28, 公開日: 2022-07-27, 最終更新日: 2024-07-03)

主引用文献

Chen, E.H.,Kao, H.W.,Lee, C.H.,Huang, J.Y.C.,Wu, K.P.,Chen, R.P.
2.2 angstrom Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108-144 Fibril Reveals an Ordered Water Channel in the Center.
J.Am.Chem.Soc., 144:13888-13894, 2022

PubMed Abstract: Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 Å based on the gold-standard Fourier shell correlation (FSC) curve. The fibril has a novel architecture that has never been found in other amyloid fibrils. Each fibril is assembled by four protofilaments (PFs) and has an ordered water channel in the center. Each protofilament contains three β-strands (125-130, 133-135, and 138-141) arranged in an "R"-shaped construct. The structural data indicate that these three β-strand segments are the most amyloidogenic region of the prion peptide/protein and might be the site of nucleation during fibrillization under conditions without denaturants.

PubMed: 35857020
DOI: 10.1021/jacs.2c05479

実験手法

ELECTRON MICROSCOPY (2.2 Å)