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| | ==Crystal structure of the flagellar cap protein flid D2-D3 domains from serratia marcescens in Space group P432== | | ==Crystal structure of the flagellar cap protein flid D2-D3 domains from serratia marcescens in Space group P432== |
| - | <StructureSection load='5xlj' size='340' side='right' caption='[[5xlj]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5xlj' size='340' side='right'caption='[[5xlj]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xlj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XLJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xlj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AR325_17470 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=615 "Bacillus marcescens" (Bizio 1823) Trevisan in de Toni and Trevisan 1889])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5xlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlj OCA], [http://pdbe.org/5xlj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xlj RCSB], [http://www.ebi.ac.uk/pdbsum/5xlj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlj 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=5xlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlj OCA], [https://pdbe.org/5xlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xlj RCSB], [https://www.ebi.ac.uk/pdbsum/5xlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0P0QFX8_SERMA A0A0P0QFX8_SERMA]] Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.[RuleBase:RU362066] | + | [https://www.uniprot.org/uniprot/A0A0P0QFX8_SERMA A0A0P0QFX8_SERMA] Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.[RuleBase:RU362066] |
| | <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 5xlj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5xlj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| | + | *[[Flagellar proteins|Flagellar proteins]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cho, S Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Hong, H J]] | + | [[Category: Serratia marcescens]] |
| - | [[Category: Song, W S]] | + | [[Category: Cho SY]] |
| - | [[Category: Yoon, S I]] | + | [[Category: Hong HJ]] |
| - | [[Category: Bacterial flagellar cap protein]] | + | [[Category: Song WS]] |
| - | [[Category: Structural protein]] | + | [[Category: Yoon SI]] |
| Structural highlights
Function
A0A0P0QFX8_SERMA Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.[RuleBase:RU362066]
Publication Abstract from PubMed
Bacterial motility is provided by the flagellum. FliD is located at the distal end of the flagellum and plays a key role in the insertion of each flagellin protein at the growing tip of the flagellar filament. Because FliD functions as an oligomer, the determination of the oligomeric state of FliD is critical to understanding the molecular mechanism of FliD-mediated flagellar growth. FliD has been shown to adopt a pentameric or a hexameric structure depending on the bacterial species. Here, we report another distinct oligomeric form of FliD based on structural and biochemical studies. The crystal structures of the D2 and D3 domains of Serratia marcescens FliD (smFliD) were determined in two crystal forms and together revealed that smFliD assembles into a tetrameric architecture that resembles a four-pointed star plate. smFliD tetramerization was also confirmed in solution by cross-linking experiments. Although smFliD oligomerizes in a head-to-tail orientation using a common primary binding interface between the D2 and D3' domains (the prime denotes the second subunit in the oligomer) similarly to other FliD orthologs, the smFliD tetramer diverges to present a unique secondary D2-D2' binding interface. Our structure-based comparative analysis of FliD suggests that bacteria have developed diverse species-specific oligomeric forms of FliD that range from tetramers to hexamers for flagellar growth.
Tetrameric structure of the flagellar cap protein FliD from Serratia marcescens.,Cho SY, Song WS, Hong HJ, Lee GS, Kang SG, Ko HJ, Kim PH, Yoon SI Biochem Biophys Res Commun. 2017 Jul 15;489(1):63-69. doi:, 10.1016/j.bbrc.2017.05.093. Epub 2017 May 18. PMID:28527888[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cho SY, Song WS, Hong HJ, Lee GS, Kang SG, Ko HJ, Kim PH, Yoon SI. Tetrameric structure of the flagellar cap protein FliD from Serratia marcescens. Biochem Biophys Res Commun. 2017 Jul 15;489(1):63-69. doi:, 10.1016/j.bbrc.2017.05.093. Epub 2017 May 18. PMID:28527888 doi:http://dx.doi.org/10.1016/j.bbrc.2017.05.093
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