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6scn

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33mer structure of the Salmonella flagella MS-ring protein FliF

Structural highlights

6scn is a 33 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLIF_SALTY The M ring may be actively involved in energy transduction.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6scn"

@@ Line 3: / Line 3: @@
 <StructureSection load='6scn' size='340' side='right'caption='[[6scn]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6scn]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6scn]] 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=6SCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C2253_19385, CET98_24800, D7F20_23315, D7H43_03010, DD95_23270, DJ388_21365, EKL42_10645 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6scn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scn OCA], [http://pdbe.org/6scn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scn RCSB], [http://www.ebi.ac.uk/pdbsum/6scn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scn ProSAT]</span></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=6scn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scn OCA], [https://pdbe.org/6scn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scn RCSB], [https://www.ebi.ac.uk/pdbsum/6scn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A0D6FLL5_SALTM A0A0D6FLL5_SALTM]] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862]
+[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 ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus typhimurium loeffler 1892]]
 [[Category: Large Structures]]
-[[Category: Deme, J C]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Fong, Y H]]
+[[Category: Deme JC]]
-[[Category: Furlong, E J]]
+[[Category: Fong YH]]
-[[Category: Johnson, S]]
+[[Category: Furlong EJ]]
-[[Category: Kuhlen, L]]
+[[Category: Johnson S]]
-[[Category: Lea, S M]]
+[[Category: Kuhlen L]]
-[[Category: C-ring]]
+[[Category: Lea SM]]
-[[Category: Flagella]]
-[[Category: Motor protein]]
-[[Category: Ms-ring]]
-[[Category: Rotor]]
-[[Category: Secretion]]

6scn

From Proteopedia

Current revision

33mer structure of the Salmonella flagella MS-ring protein FliF

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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