9JHF

Cryo-EM structure of beta-LG fibril

これはPDB形式変換不可エントリーです。

9JHF の概要

• エントリーDOI: 10.2210/pdb9jhf/pdb
• EMDBエントリー: 61480
• 分子名称: Beta-lactoglobulin fibrils (1 entity in total)
• 機能のキーワード: protein fribril, nanomaterials, protein fibril
• 由来する生物種: Bos taurus (domestic cattle)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 20646.40

構造登録者

Xu, Y.Y.,Liu, C. (登録日: 2024-09-09, 公開日: 2025-09-03)

主引用文献

Xu, Y.,Li, D.,Zhang, Y.,Zhao, Q.,Sun, B.,Liu, C.,Li, D.,Dai, B.
beta-Lactoglobulin Forms a Conserved Fibril Core That Assembles into Diverse Fibril Polymorphs.
Nano Lett., 25:3653-3661, 2025

PubMed Abstract: The β-lactoglobulin (β-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their superior cytocompatibility, chemical resilience, and mechanical characteristics. However, the precise atomic details of β-LG's fibril assembly are not understood. In this study, we utilized cryo-electron microscopy to elucidate the composition and architecture of β-LG fibrils. We discovered that the β-LG fibril was rapidly assembled after a short time incubation. Remarkably, these fibril cores were composed of the first 32 residues, forming four β-strands that adopted a serpentine arrangement into a single protofilament. This protofilament core's stability was reinforced by hydrophobic interactions. Two identical protofilaments then align to form four distinct structural polymorphs through unique interfacial configurations, which were stabilized by hydrophilic interactions, hydrogen bonding, and electrostatic forces. Our findings provide a structural framework for understanding β-LG fibril formation and pave the way for designing innovative β-LG-based nanomaterials.

PubMed: 39992798
DOI: 10.1021/acs.nanolett.5c00137

実験手法

ELECTRON MICROSCOPY (4.06 Å)