7o1q

<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='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>

== 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.

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Abrahams, J P]]

[[Category: Blum, T B]]

[[Category: DiMaio, F]]

[[Category: Farrell, D P]]

[[Category: Luo, J]]

[[Category: Wu, J]]

[[Category: Toxin]]