6sd2
From Proteopedia
(Difference between revisions)
m (Protected "6sd2" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the RBM2inner region of the Salmonella flagella MS-ring protein FliF with 21-fold symmetry applied.== | |
| + | <StructureSection load='6sd2' size='340' side='right'caption='[[6sd2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6sd2]] is a 21 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=6SD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SD2 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]] 3.1Å</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=6sd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd2 OCA], [https://pdbe.org/6sd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd2 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd2 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 6sd2" 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]] | ||
Current revision
Structure of the RBM2inner region of the Salmonella flagella MS-ring protein FliF with 21-fold symmetry applied.
| |||||||||||
