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| | <StructureSection load='5gy2' size='340' side='right'caption='[[5gy2]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5gy2' size='340' side='right'caption='[[5gy2]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gy2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacpz Bacpz] and [http://en.wikipedia.org/wiki/Bdellostoma_burgeri Bdellostoma burgeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GY2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GY2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gy2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._spizizenii_str._W23 Bacillus subtilis subsp. spizizenii str. W23], [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Eptatretus_burgeri Eptatretus burgeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GY2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VLRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7764 Bdellostoma burgeri]), hag, BSUW23_17335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=655816 BACPZ])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=5gy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gy2 OCA], [http://pdbe.org/5gy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gy2 RCSB], [http://www.ebi.ac.uk/pdbsum/5gy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gy2 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=5gy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gy2 OCA], [https://pdbe.org/5gy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gy2 RCSB], [https://www.ebi.ac.uk/pdbsum/5gy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gy2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/E0U497_BACPZ E0U497_BACPZ]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073] | + | [https://www.uniprot.org/uniprot/B3DIN1_DANRE B3DIN1_DANRE] [https://www.uniprot.org/uniprot/Q4G1L2_EPTBU Q4G1L2_EPTBU] |
| | <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: Bacpz]] | + | [[Category: Bacillus subtilis subsp. spizizenii str. W23]] |
| - | [[Category: Bdellostoma burgeri]] | + | [[Category: Danio rerio]] |
| | + | [[Category: Eptatretus burgeri]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Song, W S]] | + | [[Category: Song WS]] |
| - | [[Category: Yoon, S I]] | + | [[Category: Yoon SI]] |
| - | [[Category: Bacterial protein immune receptor]]
| + | |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
B3DIN1_DANRE Q4G1L2_EPTBU
Publication Abstract from PubMed
Flagellin is a bacterial protein that polymerizes into the flagellar filament and is essential for bacterial motility. When flagellated bacteria invade the host, flagellin is recognized by Toll-like receptor 5 (TLR5) as a pathogen invasion signal and eventually evokes the innate immune response. Here, we provide a conserved structural mechanism by which flagellins from Gram-negative gamma-proteobacteria and Gram-positive Firmicutes bacteria bind and activate TLR5. The comparative structural analysis using our crystal structure of a complex between Bacillus subtilis flagellin (bsflagellin) and TLR5 at 2.1 A resolution, combined with the alanine scanning analysis of the binding interface, reveals a common hot spot in flagellin for TLR5 activation. An arginine residue (bsflagellin R89) of the flagellin D1 domain and its adjacent residues (bsflagellin E114 and L93) constitute a hot spot that provides shape and chemical complementarity to a cavity generated by the loop of leucine-rich repeat 9 in TLR5. In addition to the flagellin D1 domain, the D0 domain also contributes to TLR5 activity through structurally dispersed regions, but not a single focal area. These results establish the groundwork for the future design of flagellin-based therapeutics.
A conserved TLR5 binding and activation hot spot on flagellin.,Song WS, Jeon YJ, Namgung B, Hong M, Yoon SI Sci Rep. 2017 Jan 20;7:40878. doi: 10.1038/srep40878. PMID:28106112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Song WS, Jeon YJ, Namgung B, Hong M, Yoon SI. A conserved TLR5 binding and activation hot spot on flagellin. Sci Rep. 2017 Jan 20;7:40878. doi: 10.1038/srep40878. PMID:28106112 doi:http://dx.doi.org/10.1038/srep40878
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