View source for 6sd1


==Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 33-fold symmetry applied==
<StructureSection load='6sd1' size='340' side='right'caption='[[6sd1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6sd1]] is a 33 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=6SD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SD1 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]] 2.6&#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=6sd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd1 OCA], [https://pdbe.org/6sd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd1 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd1 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.
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== Publication Abstract from PubMed ==
The bacterial flagellum is a complex self-assembling nanomachine that confers motility to the cell. Despite great variation across species, all flagella are ultimately constructed from a helical propeller that is attached to a motor embedded in the inner membrane. The motor consists of a series of stator units surrounding a central rotor made up of two ring complexes, the MS-ring and the C-ring. Despite many studies, high-resolution structural information is still lacking for the MS-ring of the rotor, and proposed mismatches in stoichiometry between the two rings have long provided a source of confusion for the field. Here, we present structures of the Salmonella MS-ring, revealing a high level of variation in inter- and intrachain symmetry that provides a structural explanation for the ability of the MS-ring to function as a complex and elegant interface between the two main functions of the flagellum-protein secretion and rotation.

Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation.,Johnson S, Fong YH, Deme JC, Furlong EJ, Kuhlen L, Lea SM Nat Microbiol. 2020 Jul;5(7):966-975. doi: 10.1038/s41564-020-0703-3. Epub 2020, Apr 13. PMID:32284565<ref>PMID:32284565</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6sd1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Deme JC]]
[[Category: Fong YH]]
[[Category: Furlong EJ]]
[[Category: Johnson S]]
[[Category: Kuhlen L]]
[[Category: Lea SM]]