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| | <StructureSection load='5tdy' size='340' side='right'caption='[[5tdy]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5tdy' size='340' side='right'caption='[[5tdy]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tdy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tdy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDY 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]] 2.105Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0221, Tmari_0219 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), fliG, TM_0220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdy OCA], [http://pdbe.org/5tdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdy RCSB], [http://www.ebi.ac.uk/pdbsum/5tdy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdy 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=5tdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdy OCA], [https://pdbe.org/5tdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdy RCSB], [https://www.ebi.ac.uk/pdbsum/5tdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA]] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] [[http://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | + | [https://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Blair, D F]] | + | [[Category: Blair DF]] |
| - | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
| - | [[Category: Dahlquist, F W]] | + | [[Category: Dahlquist FW]] |
| - | [[Category: Kim, E A]] | + | [[Category: Kim EA]] |
| - | [[Category: Levenson, R]] | + | [[Category: Levenson R]] |
| - | [[Category: Lynch, M J]] | + | [[Category: Lynch MJ]] |
| - | [[Category: Sircar, R]] | + | [[Category: Sircar R]] |
| - | [[Category: Flagellar motor]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Switch complex]]
| + | |
| Structural highlights
Function
Q9WY64_THEMA The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862]
Publication Abstract from PubMed
The interface between the membrane (MS) and cytoplasmic (C) rings of the bacterial flagellar motor couples torque generation to rotation within the membrane. The structure of the C-terminal helices of the integral membrane protein FliF (FliFC) bound to the N terminal domain of the switch complex protein FliG (FliGN) reveals that FliGN folds around FliFC to produce a topology that closely resembles both the middle and C-terminal domains of FliG. The interface is consistent with solution-state nuclear magnetic resonance, small-angle X-ray scattering, in vivo interaction studies, and cellular motility assays. Co-folding with FliFC induces substantial conformational changes in FliGN and suggests that FliF and FliG have the same stoichiometry within the rotor. Modeling the FliFC:FliGN complex into cryo-electron microscopy rotor density updates the architecture of the middle and upper switch complex and shows how domain shuffling of a conserved interaction module anchors the cytoplasmic rotor to the membrane.
Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.,Lynch MJ, Levenson R, Kim EA, Sircar R, Blair DF, Dahlquist FW, Crane BR Structure. 2016 Dec 31. pii: S0969-2126(16)30396-3. doi:, 10.1016/j.str.2016.12.006. PMID:28089452[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lynch MJ, Levenson R, Kim EA, Sircar R, Blair DF, Dahlquist FW, Crane BR. Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor. Structure. 2016 Dec 31. pii: S0969-2126(16)30396-3. doi:, 10.1016/j.str.2016.12.006. PMID:28089452 doi:http://dx.doi.org/10.1016/j.str.2016.12.006
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