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| | <StructureSection load='1yab' size='340' side='right'caption='[[1yab]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='1yab' size='340' side='right'caption='[[1yab]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YAB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yab]] is a 2 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=1YAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YAB FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o6a|1o6a]]</div></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]] 3.4Å</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=1yab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yab OCA], [https://pdbe.org/1yab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yab RCSB], [https://www.ebi.ac.uk/pdbsum/1yab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yab 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=1yab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yab OCA], [https://pdbe.org/1yab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yab RCSB], [https://www.ebi.ac.uk/pdbsum/1yab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yab ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0F6AJI7_THESQ A0A0F6AJI7_THESQ] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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: Brown, P N]] | + | [[Category: Brown PN]] |
| - | [[Category: Hill, C P]] | + | [[Category: Hill CP]] |
| - | [[Category: Joss, L A]] | + | [[Category: Joss LA]] |
| - | [[Category: Mathews, M A.A]] | + | [[Category: Mathews MAA]] |
| - | [[Category: Flagellar motor]]
| + | |
| - | [[Category: Flin]]
| + | |
| - | [[Category: Fliy]]
| + | |
| - | [[Category: Rotor]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Thermotoga maritima]]
| + | |
| Structural highlights
Function
A0A0F6AJI7_THESQ
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
FliN is a component of the bacterial flagellum that is present at levels of more than 100 copies and forms the bulk of the C ring, a drum-shaped structure at the inner end of the basal body. FliN interacts with FliG and FliM to form the rotor-mounted switch complex that controls clockwise-counterclockwise switching of the motor. In addition to its functions in motor rotation and switching, FliN is thought to have a role in the export of proteins that form the exterior structures of the flagellum (the rod, hook, and filament). Here, we describe the crystal structure of most of the FliN protein of Thermotoga maritima. FliN is a tightly intertwined dimer composed mostly of beta sheet. Several well-conserved hydrophobic residues form a nonpolar patch on the surface of the molecule. A mutation in the hydrophobic patch affected both flagellar assembly and switching, showing that this surface feature is important for FliN function. The association state of FliN in solution was studied by analytical ultracentrifugation, which provided clues to the higher-level organization of the protein. T. maritima FliN is primarily a dimer in solution, and T. maritima FliN and FliM together form a stable FliM(1)-FliN(4) complex. Escherichia coli FliN forms a stable tetramer in solution. The arrangement of FliN subunits in the tetramer was modeled by reference to the crystal structure of tetrameric HrcQB(C), a related protein that functions in virulence factor secretion in Pseudomonas syringae. The modeled tetramer is elongated, with approximate dimensions of 110 by 40 by 35 Angstroms, and it has a large hydrophobic cleft formed from the hydrophobic patches on the dimers. On the basis of the present data and available electron microscopic images, we propose a model for the organization of FliN subunits in the C ring.
Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima.,Brown PN, Mathews MA, Joss LA, Hill CP, Blair DF J Bacteriol. 2005 Apr;187(8):2890-902. PMID:15805535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brown PN, Mathews MA, Joss LA, Hill CP, Blair DF. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J Bacteriol. 2005 Apr;187(8):2890-902. PMID:15805535 doi:187/8/2890
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