6sd5: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6sd5 is ON HOLD
+==Structure of the RBM2 inner ring of Salmonella flagella MS-ring protein FliF with 22-fold symmetry applied==
+<StructureSection load='6sd5' size='340' side='right'caption='[[6sd5]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6sd5]] is a 22 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=6SD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SD5 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]] 3.1&#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=6sd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sd5 OCA], [https://pdbe.org/6sd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sd5 RCSB], [https://www.ebi.ac.uk/pdbsum/6sd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sd5 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6sd5" 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]]