View source for 8vid


==CW Flagellar Switch Complex with extra density - FliF, FliG, FliM, and FliN forming single subunit of the C-ring from Salmonella==
<StructureSection load='8vid' size='340' side='right'caption='[[8vid]], [[Resolution|resolution]] 5.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vid]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VID 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]] 5.9&#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=8vid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vid OCA], [https://pdbe.org/8vid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vid RCSB], [https://www.ebi.ac.uk/pdbsum/8vid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vid ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLIF_SALTY FLIF_SALTY] The M ring may be actively involved in energy transduction.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 A) and isolated C-ring in a clockwise pose alone (4.6 A) and bound to a regulator (5.9 A). Conformational differences between rotational poses include a 180 degrees shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation.

CryoEM structures reveal how the bacterial flagellum rotates and switches direction.,Singh PK, Sharma P, Afanzar O, Goldfarb MH, Maklashina E, Eisenbach M, Cecchini G, Iverson TM Nat Microbiol. 2024 May;9(5):1271-1281. doi: 10.1038/s41564-024-01674-1. Epub , 2024 Apr 17. PMID:38632342<ref>PMID:38632342</ref>

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