5gy2: Difference between revisions

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'''Unreleased structure'''


The entry 5gy2 is ON HOLD  until Paper Publication
==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. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GY2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/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>
</table>
== 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]
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5gy2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Song, W S]]
[[Category: Yoon, S I]]
[[Category: Bacterial protein immune receptor]]
[[Category: Immune system]]
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