7pq5

<table><tr><td colspan='2'>[[7pq5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PQ5 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=7pq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pq5 OCA], [https://pdbe.org/7pq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pq5 RCSB], [https://www.ebi.ac.uk/pdbsum/7pq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pq5 ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Bacteria have evolved toxins to outcompete other bacteria or to hijack host cell pathways. One broad family of bacterial polymorphic toxins gathers multidomain proteins with a modular organization, comprising a C-terminal toxin domain fused to a N-terminal domain that adapts to the delivery apparatus. Polymorphic toxins include bacteriocins, contact-dependent growth inhibition systems, and specialized Hcp, VgrG, PAAR or Rhs Type VI secretion (T6SS) components. We recently described and characterized Tre23, a toxin domain fused to a T6SS-associated Rhs protein in Photorhabdus laumondii, Rhs1. Here, we show that Rhs1 forms a complex with the T6SS spike protein VgrG and the EagR chaperone. Using truncation derivatives and cross-linking mass spectrometry, we demonstrate that VgrG-EagR-Rhs1 complex formation requires the VgrG C-terminal beta-helix and the Rhs1 N-terminal region. We then report the cryo-electron-microscopy structure of the Rhs1-EagR complex, demonstrating that the Rhs1 central region forms a beta-barrel cage-like structure that encapsulates the C-terminal toxin domain, and provide evidence for processing of the Rhs1 protein through aspartyl autoproteolysis. We propose a model for Rhs1 loading on the T6SS, transport and delivery into the target cell.

Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin.,Jurenas D, Rosa LT, Rey M, Chamot-Rooke J, Fronzes R, Cascales E Nat Commun. 2021 Dec 1;12(1):6998. doi: 10.1038/s41467-021-27388-0. PMID:34853317<ref>PMID:34853317</ref>

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

</div>

<div class="pdbe-citations 7pq5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cascales, E]]

[[Category: Chamot-Rooke, J]]

[[Category: Fronzes, R]]

[[Category: Jurenas, D]]

[[Category: Rey, M]]

[[Category: Rosa, L Talachia]]

[[Category: Tviss]]