6wxi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:59, 4 May 2022) (edit) (undo)
 
Line 1: Line 1:
==Colicin E1 fragment in nanodisc-embedded TolC==
==Colicin E1 fragment in nanodisc-embedded TolC==
-
<StructureSection load='6wxi' size='340' side='right'caption='[[6wxi]]' scene=''>
+
<StructureSection load='6wxi' size='340' side='right'caption='[[6wxi]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WXI FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6wxi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WXI FirstGlance]. <br>
-
</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=6wxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wxi OCA], [https://pdbe.org/6wxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wxi RCSB], [https://www.ebi.ac.uk/pdbsum/6wxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wxi ProSAT]</span></td></tr>
+
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6wxh|6wxh]]</div></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tolC, colE1-i, mtcB, mukA, refI, toc, weeA, b3035, JW5503 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=6wxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wxi OCA], [https://pdbe.org/6wxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wxi RCSB], [https://www.ebi.ac.uk/pdbsum/6wxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wxi ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[[https://www.uniprot.org/uniprot/TOLC_ECOLI TOLC_ECOLI]] Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.<ref>PMID:6337123</ref> <ref>PMID:11274125</ref> <ref>PMID:15228545</ref> <ref>PMID:18955484</ref> <ref>PMID:23176499</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The double membrane architecture of Gram-negative bacteria forms a barrier that is impermeable to most extracellular threats. Bacteriocin proteins evolved to exploit the accessible, surface-exposed proteins embedded in the outer membrane to deliver cytotoxic cargo. Colicin E1 is a bacteriocin produced by, and lethal to, Escherichia coli that hijacks the outer membrane proteins (OMPs) TolC and BtuB to enter the cell. Here, we capture the colicin E1 translocation domain inside its membrane receptor, TolC, by high-resolution cryo-electron microscopy to obtain the first reported structure of a bacteriocin bound to TolC. Colicin E1 binds stably to TolC as an open hinge through the TolC pore-an architectural rearrangement from colicin E1's unbound conformation. This binding is stable in live E. coli cells as indicated by single-molecule fluorescence microscopy. Finally, colicin E1 fragments binding to TolC plug the channel, inhibiting its native efflux function as an antibiotic efflux pump, and heightening susceptibility to three antibiotic classes. In addition to demonstrating that these protein fragments are useful starting points for developing novel antibiotic potentiators, this method could be expanded to other colicins to inhibit other OMP functions.
 +
 +
Colicin E1 opens its hinge to plug TolC.,Budiardjo SJ, Stevens JJ, Calkins AL, Ikujuni AP, Wimalasena VK, Firlar E, Case DA, Biteen JS, Kaelber JT, Slusky JSG Elife. 2022 Feb 24;11. pii: 73297. doi: 10.7554/eLife.73297. PMID:35199644<ref>PMID:35199644</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6wxi" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Budiardjo SJ]]
+
[[Category: Budiardjo, S J]]
-
[[Category: Firlar E]]
+
[[Category: Firlar, E]]
-
[[Category: Ikujuni AP]]
+
[[Category: Ikujuni, A P]]
-
[[Category: Kaelber JT]]
+
[[Category: Kaelber, J T]]
-
[[Category: Slusky JSG]]
+
[[Category: Slusky, J S.G]]
 +
[[Category: Antibiotic efflux]]
 +
[[Category: Bacteriocin]]
 +
[[Category: Transport protein]]

Current revision

Colicin E1 fragment in nanodisc-embedded TolC

PDB ID 6wxi

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools