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5yud

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==Flagellin derivative in complex with the NLR protein NAIP5==
==Flagellin derivative in complex with the NLR protein NAIP5==
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<StructureSection load='5yud' size='340' side='right' caption='[[5yud]], [[Resolution|resolution]] 4.28&Aring;' scene=''>
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<SX load='5yud' size='340' side='right' viewer='molstar' caption='[[5yud]], [[Resolution|resolution]] 4.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yud]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YUD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YUD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.28&#8491;</td></tr>
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<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=5yud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yud OCA], [http://pdbe.org/5yud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yud RCSB], [http://www.ebi.ac.uk/pdbsum/5yud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yud ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yud OCA], [https://pdbe.org/5yud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yud RCSB], [https://www.ebi.ac.uk/pdbsum/5yud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yud ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FLJB_SALTY FLJB_SALTY]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
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[https://www.uniprot.org/uniprot/BIR1E_MOUSE BIR1E_MOUSE] Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria such as Legionella or Salmonella. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. Prevents motor-neuron apoptosis induced by a variety of signals.<ref>PMID:21874021</ref> <ref>PMID:21918512</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nucleotide-binding domain- and leucine-rich repeat (LRR)-containing proteins (NLRs) function as intracellular immune receptors to detect the presence of pathogen- or host-derived signals. The mechanisms of how NLRs sense their ligands remain elusive. Here we report the structure of a bacterial flagellin derivative in complex with the NLR proteins NAIP5 and NLRC4 determined by cryo-electron microscopy at 4.28 A resolution. The structure revealed that the flagellin derivative forms two parallel helices interacting with multiple domains including BIR1 and LRR of NAIP5. Binding to NAIP5 results in a nearly complete burial of the flagellin derivative, thus stabilizing the active conformation of NAIP5. The extreme C-terminal side of the flagellin is anchored to a sterically constrained binding pocket of NAIP5, which likely acts as a structural determinant for discrimination of different bacterial flagellins by NAIP5, a notion further supported by biochemical data. Taken together, our results shed light on the molecular mechanisms underlying NLR ligand perception.
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Structural basis for specific flagellin recognition by the NLR protein NAIP5.,Yang X, Yang F, Wang W, Lin G, Hu Z, Han Z, Qi Y, Zhang L, Wang J, Sui SF, Chai J Cell Res. 2018 Jan;28(1):35-47. doi: 10.1038/cr.2017.148. Epub 2017 Nov 28. PMID:29182158<ref>PMID:29182158</ref>
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==See Also==
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*[[Flagellin 3D structures|Flagellin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yud" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Lin, G Z]]
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[[Category: Large Structures]]
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[[Category: Wang, W G]]
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[[Category: Mus musculus]]
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[[Category: Yang, F]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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[[Category: Yang, X R]]
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[[Category: Lin GZ]]
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[[Category: Cryo-em]]
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[[Category: Wang WG]]
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[[Category: Flagellin]]
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[[Category: Yang F]]
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[[Category: Immune system]]
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[[Category: Yang XR]]
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[[Category: Naip5]]
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[[Category: Nlrc4]]
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Current revision

Flagellin derivative in complex with the NLR protein NAIP5

5yud, resolution 4.28Å

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