6sd4: Difference between revisions
New page: '''Unreleased structure''' The entry 6sd4 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 34-fold symmetry applied== | ||
<StructureSection load='6sd4' size='340' side='right'caption='[[6sd4]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sd4]] is a 34 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=6SD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SD4 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]] 2.8Å</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=6sd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd4 OCA], [https://pdbe.org/6sd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd4 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd4 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 == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sd4" 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]] | |||
Latest revision as of 13:14, 22 May 2024
Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 34-fold symmetry appliedStructure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 34-fold symmetry applied
Structural highlights
FunctionFLIF_SALTY The M ring may be actively involved in energy transduction. Publication Abstract from PubMedThe 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. See AlsoReferences
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