View source for 7nst


==ColicinE9 partial translocation complex==
<StructureSection load='7nst' size='340' side='right'caption='[[7nst]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7nst]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NST 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]] 3.7&#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=7nst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nst OCA], [https://pdbe.org/7nst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nst RCSB], [https://www.ebi.ac.uk/pdbsum/7nst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nst ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OMPF_ECOLI OMPF_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.<ref>PMID:19721064</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria deploy weapons to kill their neighbours during competition for resources and to aid survival within microbiomes. Colicins were the first such antibacterial system identified, yet how these bacteriocins cross the outer membrane (OM) of Escherichia coli is unknown. Here, by solving the structures of translocation intermediates via cryo-EM and by imaging toxin import, we uncover the mechanism by which the Tol-dependent nuclease colicin E9 (ColE9) crosses the bacterial OM. We show that threading of ColE9's disordered N-terminal domain through two pores of the trimeric porin OmpF causes the colicin to disengage from its primary receptor, BtuB, and reorganises the translocon either side of the membrane. Subsequent import of ColE9 through the lumen of a single OmpF subunit is driven by the proton-motive force, which is delivered by the TolQ-TolR-TolA-TolB assembly. Our study answers longstanding questions, such as why OmpF is a better translocator than OmpC, and reconciles the mechanisms by which both Tol- and Ton-dependent bacteriocins cross the bacterial outer membrane.

Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.,Francis MR, Webby MN, Housden NG, Kaminska R, Elliston E, Chinthammit B, Lukoyanova N, Kleanthous C EMBO J. 2021 Nov 2;40(21):e108610. doi: 10.15252/embj.2021108610. Epub 2021 Sep , 13. PMID:34515361<ref>PMID:34515361</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7nst" style="background-color:#fffaf0;"></div>

==See Also==
*[[Colicin 3D structures|Colicin 3D structures]]
*[[Porin 3D structures|Porin 3D structures]]
*[[TolB|TolB]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Housden NG]]
[[Category: Kleanthous C]]
[[Category: Lukoyanova N]]
[[Category: Webby MN]]