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| - | ==Crystal Structure of TcdA1==
| + | #REDIRECT [[4o9y]] This PDB entry is obsolete and replaced by 4o9y |
| - | <StructureSection load='1vw2' size='340' side='right' caption='[[1vw2]], [[Resolution|resolution]] 3.50Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1vw2]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29999 Atcc 29999]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VW2 FirstGlance]. <br>
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| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o9x|4o9x]], [[4o9y|4o9y]], [[1vw1|1vw1]]</td></tr>
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| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcdA, tcdA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999])</td></tr>
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| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1vw2 PDBsum]</span></td></tr>
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| - | <table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Tripartite Tc toxin complexes of bacterial pathogens perforate the host membrane and translocate toxic enzymes into the host cell, including in humans. The underlying mechanism is complex but poorly understood. Here we report the first, to our knowledge, high-resolution structures of a TcA subunit in its prepore and pore state and of a complete 1.7 megadalton Tc complex. The structures reveal that, in addition to a translocation channel, TcA forms four receptor-binding sites and a neuraminidase-like region, which are important for its host specificity. pH-induced opening of the shell releases an entropic spring that drives the injection of the TcA channel into the membrane. Binding of TcB/TcC to TcA opens a gate formed by a six-bladed beta-propeller and results in a continuous protein translocation channel, whose architecture and properties suggest a novel mode of protein unfolding and translocation. Our results allow us to understand key steps of infections involving Tc toxins at the molecular level.
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| - | Mechanism of Tc toxin action revealed in molecular detail.,Meusch D, Gatsogiannis C, Efremov RG, Lang AE, Hofnagel O, Vetter IR, Aktories K, Raunser S Nature. 2014 Apr 3;508(7494):61-5. doi: 10.1038/nature13015. Epub 2014 Feb 23. PMID:24572368<ref>PMID:24572368</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Atcc 29999]]
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| - | [[Category: Aktories, K.]]
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| - | [[Category: Efremov, R G.]]
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| - | [[Category: Gatsogiannis, C.]]
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| - | [[Category: Hofnagel, O.]]
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| - | [[Category: Lang, A E.]]
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| - | [[Category: Meusch, D.]]
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| - | [[Category: Raunser, S.]]
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| - | [[Category: Vetter, I R.]]
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| - | [[Category: Pore-forming]]
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| - | [[Category: Tc toxin]]
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| - | [[Category: Toxin]]
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| - | [[Category: Transmembrane]]
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