9v4f
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Soy storage protein fibril (glycinin A) PM2== | |
| + | <StructureSection load='9v4f' size='340' side='right'caption='[[9v4f]], [[Resolution|resolution]] 3.52Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9v4f]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9V4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9V4F FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.52Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9v4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9v4f OCA], [https://pdbe.org/9v4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9v4f RCSB], [https://www.ebi.ac.uk/pdbsum/9v4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9v4f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLYG4_SOYBN GLYG4_SOYBN] Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, PubMed:28590128, Ref.17).<ref>PMID:22236762</ref> <ref>PMID:2485233</ref> <ref>PMID:28590128</ref> <ref>PMID:30263339</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 A) 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 pi-stacking. These atomic structures establish fundamental structure-property relationships that will inform the rational design of plant protein-based nanomaterials. | ||
| - | + | Dual Hydrophilic-Hydrophobic Core Architecture in Soy Glycinin Amyloid Fibrils Revealed by Cryo-EM.,Li S, Li S, Cheng Y, Fang Y, Cao Q, Cao Y Adv Sci (Weinh). 2025 Aug 29:e09821. doi: 10.1002/advs.202509821. PMID:40883254<ref>PMID:40883254</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cao | + | <div class="pdbe-citations 9v4f" style="background-color:#fffaf0;"></div> |
| - | [[Category: Cao | + | == References == |
| - | [[Category: Li | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glycine max]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cao Q]] | ||
| + | [[Category: Cao Y]] | ||
| + | [[Category: Li S]] | ||
Current revision
Soy storage protein fibril (glycinin A) PM2
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Categories: Glycine max | Large Structures | Cao Q | Cao Y | Li S
