View source for 5gy2


==Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5==
<StructureSection load='5gy2' size='340' side='right'caption='[[5gy2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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'>[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>
== Function ==
[https://www.uniprot.org/uniprot/B3DIN1_DANRE B3DIN1_DANRE] [https://www.uniprot.org/uniprot/Q4G1L2_EPTBU Q4G1L2_EPTBU] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:28106112</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gy2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Flagellin 3D structures|Flagellin 3D structures]]
*[[Toll-like Receptor 3D structures|Toll-like Receptor 3D structures]]
*[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. spizizenii str. W23]]
[[Category: Danio rerio]]
[[Category: Eptatretus burgeri]]
[[Category: Large Structures]]
[[Category: Song WS]]
[[Category: Yoon SI]]