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| | <StructureSection load='5xrw' size='340' side='right'caption='[[5xrw]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5xrw' size='340' side='right'caption='[[5xrw]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xrw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XRW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xrw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRW FirstGlance]. <br> |
| - | </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=5xrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrw OCA], [http://pdbe.org/5xrw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xrw RCSB], [http://www.ebi.ac.uk/pdbsum/5xrw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrw ProSAT]</span></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]] 2.5Å</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=5xrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrw OCA], [https://pdbe.org/5xrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrw RCSB], [https://www.ebi.ac.uk/pdbsum/5xrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/O25306_HELPY O25306_HELPY] |
| - | Bacterial flagella are rotary nanomachines that contribute to bacterial fitness in many settings, including host colonization. The flagellar motor relies on the multiprotein flagellar motor-switch complex to govern flagellum formation and rotational direction. Different bacteria exhibit great diversity in their flagellar motors. One such variation is exemplified by the motor-switch apparatus of the gastric pathogen Helicobacter pylori, which carries an extra switch protein, FliY, along with the more typical FliG, FliM, and FliN proteins. All switch proteins are needed for normal flagellation and motility in H. pylori, but the molecular mechanism of their assembly is unknown. To fill this gap, we examined the interactions among these proteins. We found that the C-terminal SpoA domain of FliY (FliYC) is critical to flagellation and forms heterodimeric complexes with the FliN and FliM SpoA domains, which are beta-sheet domains of type III secretion system proteins. Surprisingly, unlike in other flagellar switch systems, neither FliY nor FliN self-associated. The crystal structure of the FliYC-FliNC complex revealed a saddle-shaped structure homologous to the FliN-FliN dimer of Thermotoga maritima, consistent with a FliY-FliN heterodimer forming the functional unit. Analysis of the FliYC-FliNC interface indicated that oppositely charged residues specific to each protein drive heterodimer formation. Moreover, both FliYC-FliMC and FliYC-FliNC associated with the flagellar regulatory protein FliH, explaining their important roles in flagellation. We conclude that H. pylori uses a FliY-FliN heterodimer instead of a homodimer and creates a switch complex with SpoA domains derived from three distinct proteins.
| + | |
| - | | + | |
| - | Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system in Helicobacter pylori.,Lam KH, Xue C, Sun K, Zhang H, Lam WWL, Zhu Z, Ng JTY, Sause WE, Lertsethtakarn P, Lau KF, Ottemann KM, Au SWN J Biol Chem. 2018 Sep 7;293(36):13961-13973. doi: 10.1074/jbc.RA118.002263. Epub , 2018 Jul 10. PMID:29991595<ref>PMID:29991595</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5xrw" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Au, S W.N]] | + | [[Category: Au SWN]] |
| - | [[Category: Lam, K H]] | + | [[Category: Lam KH]] |
| - | [[Category: Xue, C]] | + | [[Category: Xue C]] |
| - | [[Category: C-ring]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Motor switch complex]]
| + | |
