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| | <SX load='5yud' size='340' side='right' viewer='molstar' caption='[[5yud]], [[Resolution|resolution]] 4.28Å' scene=''> | | <SX load='5yud' size='340' side='right' viewer='molstar' caption='[[5yud]], [[Resolution|resolution]] 4.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yud]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Salty Salty]. 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://proteopedia.org/fgij/fg.htm?mol=5YUD FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.28Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Naip5, Birc1e ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), fliC, flaF, hag, STM1959 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr> | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | + | <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 == |
| - | [[http://www.uniprot.org/uniprot/FLJB_SALTY FLJB_SALTY]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | + | [https://www.uniprot.org/uniprot/FLJB_SALTY FLJB_SALTY] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Baculoviral IAP repeat-containing protein 3D structures|Baculoviral IAP repeat-containing protein 3D structures]] | |
| | *[[Flagellin 3D structures|Flagellin 3D structures]] | | *[[Flagellin 3D structures|Flagellin 3D structures]] |
| | == References == | | == References == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Lin, G Z]] | + | [[Category: Lin GZ]] |
| - | [[Category: Wang, W G]] | + | [[Category: Wang WG]] |
| - | [[Category: Yang, F]] | + | [[Category: Yang F]] |
| - | [[Category: Yang, X R]] | + | [[Category: Yang XR]] |
| - | [[Category: Cryo-em]]
| + | |
| - | [[Category: Flagellin]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Naip5]]
| + | |
| - | [[Category: Nlrc4]]
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| Structural highlights
Function
FLJB_SALTY Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang X, Yang F, Wang W, Lin G, Hu Z, Han Z, Qi Y, Zhang L, Wang J, Sui SF, Chai J. Structural basis for specific flagellin recognition by the NLR protein NAIP5. Cell Res. 2018 Jan;28(1):35-47. doi: 10.1038/cr.2017.148. Epub 2017 Nov 28. PMID:29182158 doi:http://dx.doi.org/10.1038/cr.2017.148
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