View source for 27wr


==horse myoglobin amyloid fibril - PM1==
<StructureSection load='27wr' size='340' side='right'caption='[[27wr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[27wr]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=27WR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=27WR 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]] 2.7&#8491;</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=27wr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=27wr OCA], [https://pdbe.org/27wr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=27wr RCSB], [https://www.ebi.ac.uk/pdbsum/27wr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=27wr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The atomic architecture of apomyoglobin amyloid fibrils, despite the protein's dual distinction as the first structurally resolved protein and the paradigmatic nondisease amyloid, has remained a decades-long puzzle. Here, we identify electrostatic screening as the critical switch that enables the formation of highly ordered apomyoglobin fibrils, allowing us to determine the cryo-electron microscopy structures of three distinct polymorphs (PM1, PM2, and PM3) at 2.7 A resolution. The structures reveal a conserved "hydrophobic-in, positively charged-out" architecture, where a charged surface surrounds a tightly packed core, providing a structural explanation for salt-dependent assembly. Structural comparisons reveal a hierarchical principle of amyloid organization, in which short sequence segments retain conserved local conformations dictated by their intrinsic folding propensities, while variations in supramolecular packing give rise to polymorphic diversity. These findings establish a molecular framework for understanding electrostatically controlled self-assembly and the structural basis of amyloid polymorphism.

Myoglobin Amyloid Fibrils Reveal a Hierarchical Principle of Polymorphism and Electrostatic Self-Assembly.,Li S, Li S, Zhao Y, Fang Y, Cao Q, Cao Y Nano Lett. 2026 Jul 15;26(27):8827-8833. doi: 10.1021/acs.nanolett.6c02104. Epub , 2026 Jun 30. PMID:42378159<ref>PMID:42378159</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 27wr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Cao Q]]
[[Category: Cao Y]]
[[Category: Li S]]