6klx

<table><tr><td colspan='2'>[[6klx]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KLX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KLX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6klx OCA], [http://pdbe.org/6klx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6klx RCSB], [http://www.ebi.ac.uk/pdbsum/6klx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6klx ProSAT]</span></td></tr>

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

== Publication Abstract from PubMed ==

The iota toxin produced by Clostridium perfringens type E is a binary toxin comprising two independent polypeptides: Ia, an ADP-ribosyltransferase, and Ib, which is involved in cell binding and translocation of Ia across the cell membrane. Here we report cryo-EM structures of the translocation channel Ib-pore and its complex with Ia. The high-resolution Ib-pore structure demonstrates a similar structural framework to that of the catalytic varphi-clamp of the anthrax protective antigen pore. However, the Ia-bound Ib-pore structure shows a unique binding mode of Ia: one Ia binds to the Ib-pore, and the Ia amino-terminal domain forms multiple weak interactions with two additional Ib-pore constriction sites. Furthermore, Ib-binding induces tilting and partial unfolding of the Ia N-terminal alpha-helix, permitting its extension to the varphi-clamp gate. This new mechanism of N-terminal unfolding is crucial for protein translocation.

 

Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.,Yamada T, Yoshida T, Kawamoto A, Mitsuoka K, Iwasaki K, Tsuge H Nat Struct Mol Biol. 2020 Mar;27(3):288-296. doi: 10.1038/s41594-020-0388-6. Epub, 2020 Mar 2. PMID:32123390<ref>PMID:32123390</ref>

 

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

</div>

<references/>

[[Category: Bacillus perfringens veillon and zuber 1898]]

[[Category: Iwasaki, K]]

[[Category: Kawamoto, A]]

[[Category: Mitsuoka, K]]

[[Category: Tsuge, H]]

[[Category: Yamada, T]]

[[Category: Yoshida, T]]

[[Category: Toxin]]