6klw: Difference between revisions

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<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=6klw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6klw OCA], [http://pdbe.org/6klw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6klw RCSB], [http://www.ebi.ac.uk/pdbsum/6klw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6klw ProSAT]</span></td></tr>

</table>

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

</div>

== References ==

__TOC__

</SX>

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@@ Line 7: / Line 7: @@
 <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=6klw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6klw OCA], [http://pdbe.org/6klw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6klw RCSB], [http://www.ebi.ac.uk/pdbsum/6klw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6klw ProSAT]</span></td></tr>
 </table>
+<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>
+<div class="pdbe-citations 6klw" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </SX>