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| | ==Crystal Structure of a prokaryotic SEFIR domain== | | ==Crystal Structure of a prokaryotic SEFIR domain== |
| - | <StructureSection load='5y8f' size='340' side='right' caption='[[5y8f]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5y8f' size='340' side='right'caption='[[5y8f]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y8f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_f65185 Bacillus cereus f65185]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y8F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y8f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_F65185 Bacillus cereus F65185]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y8F FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bcere0025_60270 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=526989 Bacillus cereus F65185])</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]] 2Å</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=5y8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y8f OCA], [http://pdbe.org/5y8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y8f RCSB], [http://www.ebi.ac.uk/pdbsum/5y8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y8f 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=5y8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y8f OCA], [https://pdbe.org/5y8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y8f RCSB], [https://www.ebi.ac.uk/pdbsum/5y8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y8f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/C2XMK4_BACCE C2XMK4_BACCE] |
| - | SEFIR domain-containing proteins are crucial for mammalian adaptive immunity. As a unique intracellular signaling domain, the SEFIR-SEFIR interactions mediate physical protein-protein interactions in the immune signaling network, especially the IL-17- and IL-25-mediated pathways. However, due to the lack of structural information, the detailed molecular mechanism for SEFIR-SEFIR assembly remains unclear. In the present study, we solved the crystal structures of a prokaryotic SEFIR domain from Bacillus cereus F65185 (BcSEFIR), where the SEFIR domain is located at the N terminus. The structure of BcSEFIR revealed two radically distinct SEFIR-SEFIR interaction modes. In the asymmetric form, the C-terminal tail of one SEFIR binds to the helix alphaA and betaB-alphaB' segment of the other one, while in the symmetric form, the helices etaC and alphaE and the DE-segment compose the inter-protomer interface. The C-terminal tail of BcSEFIR, critical for asymmetric interaction, is highly conserved among the SEFIR domains of Act1 orthologs from different species, in particular three absolutely conserved residues that constitute an EXXXXPP motif. In the symmetric interaction mode, the most significant contacts made by residues on helix alphaE are highly conserved in Act1 SEFIR domains, constituted an RLI/LXE motif. The two novel SEFIR-SEFIR interaction modes might explain the structural basis for SEFIR domain-mediated complex assembly in signaling pathways.
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| - | Structure of a prokaryotic SEFIR domain reveals two novel SEFIR-SEFIR interaction modes.,Yang H, Zhu Y, Chen X, Li X, Ye S, Zhang R J Struct Biol. 2018 Mar 14. pii: S1047-8477(18)30067-4. doi:, 10.1016/j.jsb.2018.03.005. PMID:29549035<ref>PMID:29549035</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5y8f" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus cereus f65185]] | + | [[Category: Bacillus cereus F65185]] |
| - | [[Category: Yang, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Ye, S]] | + | [[Category: Yang H]] |
| - | [[Category: Zhang, R]] | + | [[Category: Ye S]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Zhang R]] |
| - | [[Category: Sefir]]
| + | [[Category: Zhu Y]] |
| - | [[Category: Signaling protein]]
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