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| | <StructureSection load='6ai0' size='340' side='right'caption='[[6ai0]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='6ai0' size='340' side='right'caption='[[6ai0]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ai0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AI0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ai0]] is a 2 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=6AI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AI0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a5i|3a5i]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></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])</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=6ai0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ai0 OCA], [https://pdbe.org/6ai0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ai0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ai0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ai0 ProSAT]</span></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=6ai0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ai0 OCA], [http://pdbe.org/6ai0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ai0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ai0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ai0 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. | + | [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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| | </div> | | </div> |
| | <div class="pdbe-citations 6ai0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ai0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Imada, K]] | + | [[Category: Imada K]] |
| - | [[Category: Kinoshita, M]] | + | [[Category: Kinoshita M]] |
| - | [[Category: Minamino, T]] | + | [[Category: Minamino T]] |
| - | [[Category: Ogawa, Y]] | + | [[Category: Ogawa Y]] |
| - | [[Category: Flagellar type iii secretion]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| 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
Bacteria use a type III protein export apparatus for construction of the flagellum, which consists of the basal body, the hook, and the filament. FlhA forms a homo-nonamer through its C-terminal cytoplasmic domains (FlhAC) and ensures the strict order of flagellar assembly. FlhAC goes through dynamic domain motions during protein export, but it remains unknown how it occurs. Here, we report that the FlhA(G368C) mutation biases FlhAC toward a closed form, thereby reducing the binding affinity of FlhAC for flagellar export chaperones in complex with their cognate filament-type substrates. The G368C mutations also restrict the conformational flexibility of a linker region of FlhA (FlhAL), suppressing FlhAC ring formation. We propose that interactions of FlhAL with its neighboring subunit converts FlhAC in the ring from a closed conformation to an open one, allowing the chaperon/substrate complexes to bind to the FlhAC ring to form the filament at the hook tip.
Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus.,Inoue Y, Ogawa Y, Kinoshita M, Terahara N, Shimada M, Kodera N, Ando T, Namba K, Kitao A, Imada K, Minamino T Structure. 2019 Apr 16. pii: S0969-2126(19)30095-4. doi:, 10.1016/j.str.2019.03.017. PMID:31031200[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Inoue Y, Ogawa Y, Kinoshita M, Terahara N, Shimada M, Kodera N, Ando T, Namba K, Kitao A, Imada K, Minamino T. Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus. Structure. 2019 Apr 16. pii: S0969-2126(19)30095-4. doi:, 10.1016/j.str.2019.03.017. PMID:31031200 doi:http://dx.doi.org/10.1016/j.str.2019.03.017
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