9V45

Soy storage protein fibril (glycinin A) PM1

Summary for 9V45

• Entry DOI: 10.2210/pdb9v45/pdb
• EMDB information: 64767
• Descriptor: Glycinin G4 (1 entity in total)
• Functional Keywords: dual hydrophilic-hydrophobic, protein fibril
• Biological source: Glycine max (soybean)
• Total number of polymer chains: 10
• Total formula weight: 638751.99

Authors

Li, S.,Cao, Q.,Cao, Y. (deposition date: 2025-05-22, release date: 2025-09-10, Last modification date: 2025-11-26)

Primary citation

Li, S.,Li, S.,Cheng, Y.,Fang, Y.,Cao, Q.,Cao, Y.
Dual Hydrophilic-Hydrophobic Core Architecture in Soy Glycinin Amyloid Fibrils Revealed by Cryo-EM.
Adv Sci, 12:e09821-e09821, 2025

PubMed Abstract: Plant-derived amyloid fibrils represent a promising class of sustainable nanomaterials outperforming their native counterparts in functionalities; however, the atomic-level structural mechanisms behind these enhancements have yet to be elucidated. Using cryo-EM, near-atomic resolution structures (3.4 and 3.5 Å) are determined for two distinct fibril polymorphs assembled in vitro from soy glycinin-A subunit. The dominant Type I fibril exhibits an unprecedented dual-core architecture, characterized by spatially segregated hydrophilic (Asp172-Asn178/Asn178'-Asp172') and hydrophobic (Val166-Ile168/Val186'-Pro184') domains, which contribute to a unique amyloid fold distinct from many known amyloid structures, including pathological and functional amyloids. In contrast, the minor Type II fibril adopts a conventional extended hydrophobic core with Tyr155-Tyr158 π-stacking. These atomic structures establish fundamental structure-property relationships that will inform the rational design of plant protein-based nanomaterials.

PubMed: 40883254
DOI: 10.1002/advs.202509821

Experimental method

ELECTRON MICROSCOPY (3.41 Å)