6h6e: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6h6e is ON HOLD
+==PTC3 holotoxin complex from Photorhabdus luminecens in prepore state (TcdA1, TcdB2, TccC3)==
+<SX load='6h6e' size='340' side='right' viewer='molstar' caption='[[6h6e]], [[Resolution|resolution]] 3.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6h6e]] is a 6 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=6H6E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6H6E FirstGlance]. <br>
+</td></tr><tr id='gene'><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]), TccC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999])</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=6h6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h6e OCA], [http://pdbe.org/6h6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h6e RCSB], [http://www.ebi.ac.uk/pdbsum/6h6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h6e ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Tc toxins secrete toxic enzymes into host cells using a unique syringe-like injection mechanism. They are composed of three subunits, TcA, TcB and TcC. TcA forms the translocation channel and the TcB-TcC heterodimer functions as a cocoon that shields the toxic enzyme. Binding of the cocoon to the channel triggers opening of the cocoon and translocation of the toxic enzyme into the channel. Here we show in atomic detail how the assembly of the three components activates the toxin. We find that part of the cocoon completely unfolds and refolds into an alternative conformation upon binding. The presence of the toxic enzyme inside the cocoon is essential for its subnanomolar binding affinity for the TcA subunit. The enzyme passes through a narrow negatively charged constriction site inside the cocoon, probably acting as an extruder that releases the unfolded protein with its C terminus first into the translocation channel.
-Authors:
+Tc toxin activation requires unfolding and refolding of a beta-propeller.,Gatsogiannis C, Merino F, Roderer D, Balchin D, Schubert E, Kuhlee A, Hayer-Hartl M, Raunser S Nature. 2018 Sep 19. pii: 10.1038/s41586-018-0556-6. doi:, 10.1038/s41586-018-0556-6. PMID:30232455<ref>PMID:30232455</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6h6e" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Atcc 29999]]
+[[Category: Large Structures]]
+[[Category: Balchin, D]]
+[[Category: Gatsogiannis, C]]
+[[Category: Hayer-Hartl, M]]
+[[Category: Kuhlee, A]]
+[[Category: Merino, F]]
+[[Category: Raunser, S]]
+[[Category: Roderer, D]]
+[[Category: Schubert, E]]
+[[Category: A-pft]]
+[[Category: Abc]]
+[[Category: Bacterial toxin]]
+[[Category: Photorhabdus]]
+[[Category: Pore forming toxin]]
+[[Category: Toxin]]
+[[Category: Translocation]]