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7una

From Proteopedia

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<StructureSection load='7una' size='340' side='right'caption='[[7una]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='7una' size='340' side='right'caption='[[7una]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7una]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UNA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7una]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobacterium_faecium Sphingobacterium faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UNA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4BW:2-AMINO-9-[(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-9-(6-AMINO-9H-PURIN-9-YL)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECIN-2-YL]-1,9-DIHYDRO-6H-PURIN-6-ONE'>4BW</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7un8|7un8]]</div></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=4BW:2-AMINO-9-[(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-9-(6-AMINO-9H-PURIN-9-YL)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECIN-2-YL]-1,9-DIHYDRO-6H-PURIN-6-ONE'>4BW</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] </span></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=7una FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7una OCA], [https://pdbe.org/7una PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7una RCSB], [https://www.ebi.ac.uk/pdbsum/7una PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7una 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=7una FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7una OCA], [https://pdbe.org/7una PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7una RCSB], [https://www.ebi.ac.uk/pdbsum/7una PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7una ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CAP12_SPHFK CAP12_SPHFK]] CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system (PubMed:32839535).<ref>PMID:32839535</ref> <ref>PMID:32877915</ref> The effector protein for this CBASS system. Upon activation by c-di-GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation. Induction in an E.coli strain that synthesizes c-di-GMP leads to significant growth inhibition. Binds c-di-GMP and 3'3'-cGAMP (3'3'-cyclic GMP-AMP), but not c-di-AMP, 2'3'-cGAMP or cUMP-AMP.<ref>PMID:32877915</ref>
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[https://www.uniprot.org/uniprot/CAP12_SPHFK CAP12_SPHFK] CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system (PubMed:32839535).<ref>PMID:32839535</ref> <ref>PMID:32877915</ref> The effector protein for this CBASS system. Upon activation by c-di-GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation. Induction in an E.coli strain that synthesizes c-di-GMP leads to significant growth inhibition. Binds c-di-GMP and 3'3'-cGAMP (3'3'-cyclic GMP-AMP), but not c-di-AMP, 2'3'-cGAMP or cUMP-AMP.<ref>PMID:32877915</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Stimulator of interferon genes (STING) is an antiviral signalling protein that is broadly conserved in both innate immunity in animals and phage defence in prokaryotes(1-4). Activation of STING requires its assembly into an oligomeric filament structure through binding of a cyclic dinucleotide(4-13), but the molecular basis of STING filament assembly and extension remains unknown. Here we use cryogenic electron microscopy to determine the structure of the active Toll/interleukin-1 receptor (TIR)-STING filament complex from a Sphingobacterium faecium cyclic-oligonucleotide-based antiphage signalling system (CBASS) defence operon. Bacterial TIR-STING filament formation is driven by STING interfaces that become exposed on high-affinity recognition of the cognate cyclic dinucleotide signal c-di-GMP. Repeating dimeric STING units stack laterally head-to-head through surface interfaces, which are also essential for human STING tetramer formation and downstream immune signalling in mammals(5). The active bacterial TIR-STING structure reveals further cross-filament contacts that brace the assembly and coordinate packing of the associated TIR NADase effector domains at the base of the filament to drive NAD(+) hydrolysis. STING interface and cross-filament contacts are essential for cell growth arrest in vivo and reveal a stepwise mechanism of activation whereby STING filament assembly is required for subsequent effector activation. Our results define the structural basis of STING filament formation in prokaryotic antiviral signalling.
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Cryo-EM structure of an active bacterial TIR-STING filament complex.,Morehouse BR, Yip MCJ, Keszei AFA, McNamara-Bordewick NK, Shao S, Kranzusch PJ Nature. 2022 Jul 20. pii: 10.1038/s41586-022-04999-1. doi:, 10.1038/s41586-022-04999-1. PMID:35859168<ref>PMID:35859168</ref>
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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 7una" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Keszei, A F.A]]
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[[Category: Sphingobacterium faecium]]
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[[Category: Kranzusch, P J]]
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[[Category: Keszei AFA]]
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[[Category: McNamara-Bordewick, N K]]
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[[Category: Kranzusch PJ]]
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[[Category: Morehouse, B R]]
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[[Category: McNamara-Bordewick NK]]
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[[Category: Shao, S]]
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[[Category: Morehouse BR]]
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[[Category: Yip, M C.J]]
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[[Category: Shao S]]
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[[Category: Antiviral protein]]
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[[Category: Yip MCJ]]
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[[Category: Bacterial]]
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[[Category: Filament]]
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[[Category: Sting]]
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Current revision

SfSTING with cGAMP (masked)

PDB ID 7una

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