6sd3: Difference between revisions
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<StructureSection load='6sd3' size='340' side='right'caption='[[6sd3]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6sd3' size='340' side='right'caption='[[6sd3]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6sd3]] is a 34 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6sd3]] 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=6SD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SD3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</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=6sd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd3 OCA], [https://pdbe.org/6sd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd3 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd3 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=6sd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd3 OCA], [https://pdbe.org/6sd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd3 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Deme | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | ||
[[Category: Fong | [[Category: Deme JC]] | ||
[[Category: Furlong | [[Category: Fong YH]] | ||
[[Category: Johnson | [[Category: Furlong EJ]] | ||
[[Category: Kuhlen | [[Category: Johnson S]] | ||
[[Category: Lea | [[Category: Kuhlen L]] | ||
[[Category: Lea SM]] | |||
Latest revision as of 13:14, 22 May 2024
34mer structure of the Salmonella flagella MS-ring protein FliF34mer structure of the Salmonella flagella MS-ring protein FliF
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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