9IAH
Structure of beta-lactoglobulin fibril
Summary for 9IAH
| Entry DOI | 10.2210/pdb9iah/pdb |
| EMDB information | 52781 |
| Descriptor | Beta-lactoglobulin (1 entity in total) |
| Functional Keywords | whey protein, nutrient transport, amyloid fibrillation, cross-beta structure, nanomaterial, biosynthetic protein |
| Biological source | Bos taurus (domestic cattle) |
| Total number of polymer chains | 5 |
| Total formula weight | 18136.16 |
| Authors | Sternke-Hoffmann, R.,Rhyner, D.,Qureshi, B.,Riek, R.,Greenwald, J.,Luo, J. (deposition date: 2025-02-10, release date: 2025-03-05, Last modification date: 2025-11-26) |
| Primary citation | Sternke-Hoffmann, R.,Rhyner, D.,Terashi, G.,Qureshi, B.M.,Riek, R.,Greenwald, J.,Kihara, D.,Lutz-Bueno, V.,Luo, J. Structural Insights and Functional Dynamics of beta-Lactoglobulin Fibrils. Nano Lett., 25:16146-16153, 2025 Cited by PubMed Abstract: Amyloid fibrils from β-lactoglobulin (β-LG), a major whey protein, have attracted interest for nanotechnology due to their biocompatibility, tunable surface chemistry, and ability to bind functional molecules. They serve as scaffolds for metal nanoparticle synthesis, carriers for bioactive compounds, and building blocks for nanomaterials with tailored mechanical and optical properties. However, their dynamic architecture remains incompletely understood, limiting their rational design. Here, we combine cryo-electron microscopy (cryo-EM), small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations to investigate β-LG fibrils formed under mildly denaturing conditions. Cryo-EM reveals a monomeric polymorph with a conserved core (Leu1-Ala34) and a disordered "fuzzy coat". Flexible domains were modeled and evaluated by MD, identifying one stable conformation (Asn90-Thr97). The ionic strength reduced the coat flexibility and promoted iron binding, suggesting environmental responsiveness. These findings link fibril flexibility to functional potential, offering mechanistic insight into engineering β-LG-based nanomaterials. PubMed: 41129746DOI: 10.1021/acs.nanolett.5c04125 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.17 Å) |
Structure validation
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