6ch2: Difference between revisions
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<StructureSection load='6ch2' size='340' side='right'caption='[[6ch2]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6ch2' size='340' side='right'caption='[[6ch2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ch2]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ch2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi Salmonella enterica subsp. enterica serovar Typhi] and [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=6CH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CH2 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">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ch2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ch2 OCA], [https://pdbe.org/6ch2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ch2 RCSB], [https://www.ebi.ac.uk/pdbsum/6ch2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ch2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FLHA_SALTY FLHA_SALTY] Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. | ||
<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: | [[Category: Salmonella enterica subsp. enterica serovar Typhi]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: | [[Category: Kalodimos CG]] | ||
[[Category: | [[Category: Shi K]] | ||
[[Category: | [[Category: Xing Q]] | ||
Latest revision as of 18:04, 4 October 2023
Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complexCrystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex
Structural highlights
FunctionFLHA_SALTY Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. Publication Abstract from PubMedThe flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate. Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system.,Xing Q, Shi K, Portaliou A, Rossi P, Economou A, Kalodimos CG Nat Commun. 2018 May 2;9(1):1773. doi: 10.1038/s41467-018-04137-4. PMID:29720631[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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