6WL8

Cryo-EM of Form 2 peptide filament

これはPDB形式変換不可エントリーです。

6WL8 の概要

• エントリーDOI: 10.2210/pdb6wl8/pdb
• EMDBエントリー: 21812 21813 21814 21815 21816 21817 21818
• 分子名称: Form 2 peptide (1 entity in total)
• 機能のキーワード: filament, self-assembly peptide filament, cryo-em, protein fibril
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 106
• 化学式量合計: 338960.55

構造登録者

Wang, F.,Gnewou, O.M.,Xu, C.,Su, Z.,Egelman, E.H.,Conticello, V.P. (登録日: 2020-04-18, 公開日: 2020-12-02, 最終更新日: 2025-06-04)

主引用文献

Wang, F.,Gnewou, O.,Modlin, C.,Beltran, L.C.,Xu, C.,Su, Z.,Juneja, P.,Grigoryan, G.,Egelman, E.H.,Conticello, V.P.
Structural analysis of cross alpha-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.
Nat Commun, 12:407-407, 2021

PubMed Abstract: The exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.

PubMed: 33462223
DOI: 10.1038/s41467-020-20689-w

実験手法

ELECTRON MICROSCOPY (4.1 Å)