View source for 7kal


==Cryo-EM structure of the Sec complex from T. lanuginosus, wild-type, class with Sec62, plug-open conformation==
<StructureSection load='7kal' size='340' side='right'caption='[[7kal]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7kal]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KAL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</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=7kal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kal OCA], [https://pdbe.org/7kal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kal RCSB], [https://www.ebi.ac.uk/pdbsum/7kal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kal ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many proteins are transported into the endoplasmic reticulum by the universally conserved Sec61 channel. Post-translational transport requires two additional proteins, Sec62 and Sec63, but their functions are poorly defined. In the present study, we determined cryo-electron microscopy (cryo-EM) structures of several variants of Sec61-Sec62-Sec63 complexes from Saccharomyces cerevisiae and Thermomyces lanuginosus and show that Sec62 and Sec63 induce opening of the Sec61 channel. Without Sec62, the translocation pore of Sec61 remains closed by the plug domain, rendering the channel inactive. We further show that the lateral gate of Sec61 must first be partially opened by interactions between Sec61 and Sec63 in cytosolic and luminal domains, a simultaneous disruption of which completely closes the channel. The structures and molecular dynamics simulations suggest that Sec62 may also prevent lipids from invading the channel through the open lateral gate. Our study shows how Sec63 and Sec62 work together in a hierarchical manner to activate Sec61 for post-translational protein translocation.

Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62.,Itskanov S, Kuo KM, Gumbart JC, Park E Nat Struct Mol Biol. 2021 Feb;28(2):162-172. doi: 10.1038/s41594-020-00541-x. , Epub 2021 Jan 4. PMID:33398175<ref>PMID:33398175</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomyces lanuginosus]]
[[Category: Itskanov S]]
[[Category: Park E]]