|
|
| Line 3: |
Line 3: |
| | <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 [http://en.wikipedia.org/wiki/"bacillus_typhi"_schroeter_1886 "bacillus typhi" schroeter 1886] and [http://en.wikipedia.org/wiki/Salty Salty]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CH2 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flhA, STM1913 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY]), fliT, STY2170, t0915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90370 "Bacillus typhi" Schroeter 1886])</td></tr> | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ch2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ch2 OCA], [http://pdbe.org/6ch2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ch2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ch2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ch2 ProSAT]</span></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=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 == |
| - | [[http://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. [[http://www.uniprot.org/uniprot/FLID_SALTY FLID_SALTY]] Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. | + | [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 == |
| Line 26: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhi schroeter 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhi]] |
| - | [[Category: Kalodimos, C G]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Shi, K]] | + | [[Category: Kalodimos CG]] |
| - | [[Category: Xing, Q]] | + | [[Category: Shi K]] |
| - | [[Category: Flagellar]] | + | [[Category: Xing Q]] |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
The 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 Also
References
- ↑ Xing Q, Shi K, Portaliou A, Rossi P, Economou A, Kalodimos CG. Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. Nat Commun. 2018 May 2;9(1):1773. doi: 10.1038/s41467-018-04137-4. PMID:29720631 doi:http://dx.doi.org/10.1038/s41467-018-04137-4
|
