8b3a
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==catalytic amyloid fibril formed by Ac-LHLHLRL-amide== | |
| + | <StructureSection load='8b3a' size='340' side='right'caption='[[8b3a]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8b3a]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B3A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=8b3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b3a OCA], [https://pdbe.org/8b3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b3a RCSB], [https://www.ebi.ac.uk/pdbsum/8b3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b3a ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction. In this study we used cryo-electron microcopy to analyze the amyloid fibril structure and the catalytic center of amyloid fibrils that hydrolyze ester bonds. Our findings show that catalytic amyloid fibrils are polymorphic and consist of similarly structured, zipper-like building blocks that consist of mated cross-beta sheets. These building blocks define the fibril core, which is decorated by a peripheral leaflet of peptide molecules. The observed structural arrangement differs from previously described catalytic amyloid fibrils and yielded a new model of the catalytic center. | ||
| - | + | Cryo-EM structure of a catalytic amyloid fibril.,Heerde T, Bansal A, Schmidt M, Fandrich M Sci Rep. 2023 Mar 11;13(1):4070. doi: 10.1038/s41598-023-30711-y. PMID:36906667<ref>PMID:36906667</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8b3a" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Heerde | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Faendrich M]] | ||
| + | [[Category: Heerde T]] | ||
| + | [[Category: Schmidt M]] | ||
Revision as of 06:26, 7 April 2023
catalytic amyloid fibril formed by Ac-LHLHLRL-amide
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