7o1q: Difference between revisions
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==Amyloid beta oligomer displayed on the alpha hemolysin scaffold== | ==Amyloid beta oligomer displayed on the alpha hemolysin scaffold== | ||
<StructureSection load='7o1q' size='340' side='right'caption='[[7o1q]]' scene=''> | <StructureSection load='7o1q' size='340' side='right'caption='[[7o1q]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O1Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[7o1q]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O1Q FirstGlance]. <br> | ||
</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=7o1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1q OCA], [https://pdbe.org/7o1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1q RCSB], [https://www.ebi.ac.uk/pdbsum/7o1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1q ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hly, hla ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=7o1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1q OCA], [https://pdbe.org/7o1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1q RCSB], [https://www.ebi.ac.uk/pdbsum/7o1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1q ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/HLA_STAAU HLA_STAAU]] Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Amyloid-beta peptide (Abeta) oligomers are pathogenic species of amyloid aggregates in Alzheimer's disease. Like certain protein toxins, Abeta oligomers permeabilize cellular membranes, presumably through a pore formation mechanism. Due to their structural and stoichiometric heterogeneity, the structure of these pores remains to be characterized. We studied a functional Abeta42-pore equivalent, created by fusing Abeta42 to the oligomerizing, soluble domain of the alpha-hemolysin (alphaHL) toxin. Our data reveal Abeta42-alphaHL oligomers to share major structural, functional and biological properties with wild-type Abeta42-pores. Single-particle cryo-EM analysis of Abeta42-alphaHL oligomers (with an overall resolution of 3.3 A) reveals the Abeta42-pore region to be intrinsically flexible. We anticipate that the Abeta42-alphaHL oligomers will allow studying many of the features of the wild type amyloid oligomers that cannot be studied otherwise, and may represent a highly specific antigen for the development of immuno-base diagnostics and therapies. | |||
Cryo-electron microscopy imaging of Alzheimer's amyloid-beta 42 oligomer displayed on a functionally and structurally relevant scaffold.,Wu J, Blum TB, Farrell DP, DiMaio F, Abrahams JP, Luo J Angew Chem Int Ed Engl. 2021 May 27. doi: 10.1002/anie.202104497. PMID:34042235<ref>PMID:34042235</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7o1q" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abrahams | [[Category: Abrahams, J P]] | ||
[[Category: Blum | [[Category: Blum, T B]] | ||
[[Category: DiMaio F]] | [[Category: DiMaio, F]] | ||
[[Category: Farrell | [[Category: Farrell, D P]] | ||
[[Category: Luo J]] | [[Category: Luo, J]] | ||
[[Category: Wu J]] | [[Category: Wu, J]] | ||
[[Category: Alpha hemolysin]] | |||
[[Category: Alzheimer's disease]] | |||
[[Category: Amyloid beta oligomer]] | |||
[[Category: Toxin]] | |||
