7bgl: Difference between revisions
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==== | ==Salmonella LP ring 26 mer refined in C26 map== | ||
<StructureSection load='7bgl' size='340' side='right'caption='[[7bgl]]' scene=''> | <StructureSection load='7bgl' size='340' side='right'caption='[[7bgl]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7bgl]] is a 78 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BGL FirstGlance]. <br> | ||
</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=7bgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bgl OCA], [https://pdbe.org/7bgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bgl RCSB], [https://www.ebi.ac.uk/pdbsum/7bgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bgl ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLW:(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4,5-bis(oxidanyl)oxane-2-carboxylic+acid'>TLW</scene>, <scene name='pdbligand=TQN:[(3~{R})-1-[[(2~{R},3~{R},4~{R},5~{S},6~{R})-6-[[(2~{R},3~{R},4~{R},5~{S},6~{R})-3-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-(hydroxymethyl)-5-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]oxymethyl]-5-oxidanyl-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-2-phosphonooxy-oxan-3-yl]amino]-1-oxidanylidene-tetradecan-3-yl]+hexadecanoate'>TQN</scene></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=7bgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bgl OCA], [https://pdbe.org/7bgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bgl RCSB], [https://www.ebi.ac.uk/pdbsum/7bgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bgl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/FLGI_SALTY FLGI_SALTY] Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the inner membrane to the micrometre-long flagellar filament that powers bacterial swimming in viscous fluids(1-3). Here, we present structures of the intact Salmonella flagellar basal body(4), encompassing the inner membrane rotor, drive shaft and outer-membrane bushing, solved using cryo-electron microscopy to resolutions of 2.2-3.7 A. The structures reveal molecular details of how 173 protein molecules of 13 different types assemble into a complex spanning two membranes and a cell wall. The helical drive shaft at one end is intricately interwoven with the rotor component with both the export gate complex and the proximal rod forming interactions with the MS-ring. At the other end, the drive shaft distal rod passes through the LP-ring bushing complex, which functions as a molecular bearing anchored in the outer membrane through interactions with the lipopolysaccharide. The in situ structure of a protein complex capping the drive shaft provides molecular insights into the assembly process of this molecular machine. | |||
Molecular structure of the intact bacterial flagellar basal body.,Johnson S, Furlong EJ, Deme JC, Nord AL, Caesar JJE, Chevance FFV, Berry RM, Hughes KT, Lea SM Nat Microbiol. 2021 Apr 30. pii: 10.1038/s41564-021-00895-y. doi:, 10.1038/s41564-021-00895-y. PMID:33931760<ref>PMID:33931760</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7bgl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: Furlong E]] | |||
[[Category: Johnson S]] | |||
[[Category: Lea SM]] | |||
Latest revision as of 12:21, 9 October 2024
Salmonella LP ring 26 mer refined in C26 mapSalmonella LP ring 26 mer refined in C26 map
Structural highlights
FunctionFLGI_SALTY Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Publication Abstract from PubMedThe bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the inner membrane to the micrometre-long flagellar filament that powers bacterial swimming in viscous fluids(1-3). Here, we present structures of the intact Salmonella flagellar basal body(4), encompassing the inner membrane rotor, drive shaft and outer-membrane bushing, solved using cryo-electron microscopy to resolutions of 2.2-3.7 A. The structures reveal molecular details of how 173 protein molecules of 13 different types assemble into a complex spanning two membranes and a cell wall. The helical drive shaft at one end is intricately interwoven with the rotor component with both the export gate complex and the proximal rod forming interactions with the MS-ring. At the other end, the drive shaft distal rod passes through the LP-ring bushing complex, which functions as a molecular bearing anchored in the outer membrane through interactions with the lipopolysaccharide. The in situ structure of a protein complex capping the drive shaft provides molecular insights into the assembly process of this molecular machine. Molecular structure of the intact bacterial flagellar basal body.,Johnson S, Furlong EJ, Deme JC, Nord AL, Caesar JJE, Chevance FFV, Berry RM, Hughes KT, Lea SM Nat Microbiol. 2021 Apr 30. pii: 10.1038/s41564-021-00895-y. doi:, 10.1038/s41564-021-00895-y. PMID:33931760[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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