View source for 8ftx


==FlgN-FliJ fusion complex==
<StructureSection load='8ftx' size='340' side='right'caption='[[8ftx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ftx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FTX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8ftx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ftx OCA], [https://pdbe.org/8ftx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ftx RCSB], [https://www.ebi.ac.uk/pdbsum/8ftx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ftx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A5K1US31_SALTM A0A5K1US31_SALTM] Required for the efficient initiation of filament assembly.[ARBA:ARBA00002397][https://www.uniprot.org/uniprot/A0A5K1UBM0_SALTM A0A5K1UBM0_SALTM] Flagellar protein that affects chemotactic events.[PIRNR:PIRNR019404]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The flagellum is a sophisticated nanomachine responsible for motility in Gram-negative bacteria. Flagellar assembly is a strictly choreographed process, in which the motor and export gate are formed first, followed by the extracellular propeller structure. Extracellular flagellar components are escorted to the export gate by dedicated molecular chaperones for secretion and self-assembly at the apex of the emerging structure. The detailed mechanisms of chaperone-substrate trafficking at the export gate remain poorly understood. Here, we structurally characterized the interaction of Salmonella enterica late-stage flagellar chaperones FliT and FlgN with the export controller protein FliJ. Previous studies showed that FliJ is absolutely required for flagellar assembly since its interaction with chaperone-client complexes controls substrate delivery to the export gate. Our biophysical and cell-based data show that FliT and FlgN bind FliJ cooperatively, with high affinity and on specific sites. Chaperone binding completely disrupts the FliJ coiled-coil structure and alters its interactions with the export gate. We propose that FliJ aids the release of substrates from the chaperone and forms the basis of chaperone recycling during late-stage flagellar assembly.

Chaperone Recycling in Late-Stage Flagellar Assembly.,Rossi P, Xing Q, Bini E, Portaliou AG, Clay MC, Warren EM, Khanra NK, Economou A, Kalodimos CG J Mol Biol. 2023 Mar 1:167954. doi: 10.1016/j.jmb.2023.167954. PMID:37330284<ref>PMID:37330284</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ftx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Kalodimos CG]]
[[Category: Rossi P]]