9V4F
Soy storage protein fibril (glycinin A) PM2
Summary for 9V4F
| Entry DOI | 10.2210/pdb9v4f/pdb |
| EMDB information | 64778 |
| Descriptor | Glycinin G4 (1 entity in total) |
| Functional Keywords | soy storage protein fibril, protein fibril |
| Biological source | Glycine max (soybean) |
| Total number of polymer chains | 10 |
| Total formula weight | 638751.99 |
| Authors | |
| 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, :e09821-e09821, 2025 Cited by 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: 40883254DOI: 10.1002/advs.202509821 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.52 Å) |
Structure validation
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