8ucs
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the flagellar MotAB stator bound to FliG== | |
| + | <StructureSection load='8ucs' size='340' side='right'caption='[[8ucs]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ucs]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_sporogenes Clostridium sporogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UCS 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]] 2.4Å</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=8ucs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ucs OCA], [https://pdbe.org/8ucs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ucs RCSB], [https://www.ebi.ac.uk/pdbsum/8ucs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ucs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1V9IL35_CLOSG A0A1V9IL35_CLOSG] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar filament. Rotation is bi-directional, with binding of a cytoplasmic chemotactic response regulator controlling reversal, though the structural and mechanistic bases for rotational switching are not well understood. Here we present cryoelectron microscopy structures of intact Salmonella flagellar basal bodies (3.2-5.5 A), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180 degrees movements of both the N- and C-terminal domains of the FliG protein, which, when combined with a high-resolution cryoelectron microscopy structure of the MotA(5)B(2) stator, show that the stator shifts from the outside to the inside of the C-ring. This enables rotational switching and reveals how uni-directional ion flow across the inner membrane is used to accomplish bi-directional rotation of the flagellum. | ||
| - | + | Structural basis of directional switching by the bacterial flagellum.,Johnson S, Deme JC, Furlong EJ, Caesar JJE, Chevance FFV, Hughes KT, Lea SM Nat Microbiol. 2024 May;9(5):1282-1292. doi: 10.1038/s41564-024-01630-z. Epub , 2024 Mar 8. PMID:38459206<ref>PMID:38459206</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8ucs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium sporogenes]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Deme JC]] | ||
| + | [[Category: Johnson S]] | ||
| + | [[Category: Lea SM]] | ||
Current revision
Cryo-EM structure of the flagellar MotAB stator bound to FliG
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