|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5h5v' size='340' side='right'caption='[[5h5v]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5h5v' size='340' side='right'caption='[[5h5v]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h5v]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H5V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h5v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H5V 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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h5s|5h5s]], [[5h5w|5h5w]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=5h5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5v OCA], [https://pdbe.org/5h5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h5v RCSB], [https://www.ebi.ac.uk/pdbsum/5h5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5v OCA], [http://pdbe.org/5h5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h5v RCSB], [http://www.ebi.ac.uk/pdbsum/5h5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A094VPA5_ECOLX A0A094VPA5_ECOLX]] 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/FLID_ECOLI FLID_ECOLI] Required for the 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 27: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cho, S Y]] | + | [[Category: Cho SY]] |
| - | [[Category: Hong, H J]] | + | [[Category: Hong HJ]] |
| - | [[Category: Song, W S]] | + | [[Category: Song WS]] |
| - | [[Category: Yoon, S I]] | + | [[Category: Yoon SI]] |
| - | [[Category: Bacterial flagellar cap protein]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
FLID_ECOLI Required for the 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.
Publication Abstract from PubMed
FliD is a self-oligomerizing structural protein that caps the growing end of the bacterial flagellar filament. FliD also plays a key role in the flagellar system by continuously adding a new flagellin protein to the tip of the filament. To structurally characterize FliD oligomerization and to provide a FliD-mediated flagellin polymerization mechanism, we have determined the crystal structures of FliD proteins from Escherichia coli and Salmonella enterica serovar Typhimurium (ecFliD and stFliD, respectively). ecFliD consists of three domains (D1, D2, and D3) and forms a hexamer plate of the D2 and D3 domains that resembles a six-pointed star with legs consisting of the D1 domain. In contrast, the D2 and D3 domains of stFliD assemble into a pentamer as a five-pointed star plate. Despite their distinct oligomeric states, ecFliD and stFliD engage a common molecular surface for oligomerization. FliD also features interdomain and intersubunit flexibility, suggesting that FliD reorganizes its domains and adjacent subunits depending on the FliD binding partner. The similarity of the FliD shape to flagellin and the structural dynamics of FliD led us to propose a FliD-catalyzed filament elongation mechanism. In this model, FliD occupies a position in place of a nascent flagellin until the flagellin reaches the growing end of the filament, and then, FliD moves aside to repeat the positional replacement.
Self-Oligomerizing Structure of the Flagellar Cap Protein FliD and Its Implication in Filament Assembly.,Song WS, Cho SY, Hong HJ, Park SC, Yoon SI J Mol Biol. 2017 Feb 6. pii: S0022-2836(17)30065-7. doi:, 10.1016/j.jmb.2017.02.001. PMID:28179186[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Song WS, Cho SY, Hong HJ, Park SC, Yoon SI. Self-Oligomerizing Structure of the Flagellar Cap Protein FliD and Its Implication in Filament Assembly. J Mol Biol. 2017 Feb 6. pii: S0022-2836(17)30065-7. doi:, 10.1016/j.jmb.2017.02.001. PMID:28179186 doi:http://dx.doi.org/10.1016/j.jmb.2017.02.001
|
