6ek7: Difference between revisions

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'''Unreleased structure'''


The entry 6ek7 is ON HOLD
==YaxA from Yersinia enterocolitica==
<StructureSection load='6ek7' size='340' side='right' caption='[[6ek7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ek7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EK7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EK7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ek7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ek7 OCA], [http://pdbe.org/6ek7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ek7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ek7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ek7 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary alpha-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA-YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of alpha-PFTs, highlighting diverse pore architectures.


Authors: Braeuning, B., Groll, M.
Structure and mechanism of the two-component alpha-helical pore-forming toxin YaxAB.,Brauning B, Bertosin E, Praetorius F, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M Nat Commun. 2018 May 4;9(1):1806. doi: 10.1038/s41467-018-04139-2. PMID:29728606<ref>PMID:29728606</ref>


Description: YaxA from Yersinia enterocolitica
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6ek7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Braeuning, B]]
[[Category: Braeuning, B]]
[[Category: Groll, M]]
[[Category: Groll, M]]
[[Category: Adventitious membrane protein]]
[[Category: Alpha-helical]]
[[Category: Membrane protein]]
[[Category: Pathogen]]
[[Category: Pore forming toxin]]

Revision as of 05:34, 16 May 2018

YaxA from Yersinia enterocolitica

6ek7, resolution 1.80Å

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