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| | <StructureSection load='3w1e' size='340' side='right'caption='[[3w1e]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3w1e' size='340' side='right'caption='[[3w1e]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"oceanomonas_alginolytica"_miyamoto_et_al._1961 "oceanomonas alginolytica" miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_alginolyticus Vibrio alginolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1E FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flgT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=663 "Oceanomonas alginolytica" Miyamoto et al. 1961])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3w1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1e OCA], [https://pdbe.org/3w1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1e RCSB], [https://www.ebi.ac.uk/pdbsum/3w1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1e 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=3w1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1e OCA], [https://pdbe.org/3w1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1e RCSB], [https://www.ebi.ac.uk/pdbsum/3w1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D9N551_VIBAL D9N551_VIBAL] |
| | <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: Oceanomonas alginolytica miyamoto et al. 1961]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Homma, M]] | + | [[Category: Vibrio alginolyticus]] |
| - | [[Category: Imada, K]] | + | [[Category: Homma M]] |
| - | [[Category: Sakuma, M]] | + | [[Category: Imada K]] |
| - | [[Category: Terashima, H]] | + | [[Category: Sakuma M]] |
| - | [[Category: H-ring formation]]
| + | [[Category: Terashima H]] |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: The flagellar basal body]]
| + | |
| Structural highlights
Function
D9N551_VIBAL
Publication Abstract from PubMed
Flagellar motility is a key factor for bacterial survival and growth in fluctuating environments. The polar flagellum of a marine bacterium, Vibrio alginolyticus, is driven by sodium ion influx and rotates approximately six times faster than the proton-driven motor of Escherichia coli. The basal body of the sodium motor has two unique ring structures, the T ring and the H ring. These structures are essential for proper assembly of the stator unit into the basal body and to stabilize the motor. FlgT, which is a flagellar protein specific for Vibrio sp., is required to form and stabilize both ring structures. Here, we report the crystal structure of FlgT at 2.0-A resolution. FlgT is composed of three domains, the N-terminal domain (FlgT-N), the middle domain (FlgT-M), and the C-terminal domain (FlgT-C). FlgT-M is similar to the N-terminal domain of TolB, and FlgT-C resembles the N-terminal domain of FliI and the alpha/beta subunits of F1-ATPase. To elucidate the role of each domain, we prepared domain deletion mutants of FlgT and analyzed their effects on the basal-body ring formation. The results suggest that FlgT-N contributes to the construction of the H-ring structure, and FlgT-M mediates the T-ring association on the LP ring. FlgT-C is not essential but stabilizes the H-ring structure. On the basis of these results, we propose an assembly mechanism for the basal-body rings and the stator units of the sodium-driven flagellar motor.
Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT.,Terashima H, Li N, Sakuma M, Koike M, Kojima S, Homma M, Imada K Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):6133-8. doi:, 10.1073/pnas.1222655110. Epub 2013 Mar 25. PMID:23530206[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Terashima H, Li N, Sakuma M, Koike M, Kojima S, Homma M, Imada K. Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):6133-8. doi:, 10.1073/pnas.1222655110. Epub 2013 Mar 25. PMID:23530206 doi:10.1073/pnas.1222655110
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