7un9 - Revision history

OCA at 09:38, 14 February 2024

OCA — Wed, 14 Feb 2024 09:38:45 GMT

←Older revision		Revision as of 09:38, 14 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7un9]] is a 12 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=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7un9]] is a 12 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=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</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]] 3.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></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=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 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=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	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.	+
-		+
-	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>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7un9" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:58, 7 September 2022

OCA — Wed, 07 Sep 2022 18:58:27 GMT

←Older revision		Revision as of 18:58, 7 September 2022
Line 9:		Line 9:
	== Function ==		== Function ==
	[[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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.
		+
		+	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>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7un9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:49, 7 September 2022

OCA — Wed, 07 Sep 2022 16:49:20 GMT

←Older revision		Revision as of 16:49, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='7un9' size='340' side='right'caption='[[7un9]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='7un9' size='340' side='right'caption='[[7un9]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7un9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7un9]] is a 12 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=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></td></tr>
-	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
-	<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>
-	<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>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 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=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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>	+	[[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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	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.	+
-		+
-	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>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7un9" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 14:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Keszei~~, A F.A~~]]	+	[[Category: Sphingobacterium faecium]]
-	[[Category: Kranzusch~~, P J~~]]	+	[[Category: Keszei AFA]]
-	[[Category: McNamara-Bordewick~~, N K~~]]	+	[[Category: Kranzusch PJ]]
-	[[Category: Morehouse~~, B R~~]]	+	[[Category: McNamara-Bordewick NK]]
-	[[Category: Shao, S]]	+	[[Category: Morehouse BR]]
-	[[Category: Yip~~, M C.J]]~~	+	[[Category: Shao S]]
-	~~[[Category: Antiviral protein]]~~	+	[[Category: Yip MCJ]]
-	~~[[Category: Bacterial]]~~	+
-	~~[[Category: Filament]]~~	+
-	~~[[Category: Sting~~]]	+

OCA at 05:03, 3 August 2022

OCA — Wed, 03 Aug 2022 05:03:46 GMT

←Older revision		Revision as of 05:03, 3 August 2022
Line 1:		Line 1:

	==SfSTING with c-di-GMP double fiber==		==SfSTING with c-di-GMP double fiber==
-	<StructureSection load='7un9' size='340' side='right'caption='[[7un9]]' scene=''>	+	<StructureSection load='7un9' size='340' side='right'caption='[[7un9]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7un9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>
-	</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=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
		+	<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>
		+	<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>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.
		+
		+	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>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7un9" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Keszei ~~AFA~~]]	+	[[Category: Keszei, A F.A]]
-	[[Category: Kranzusch PJ]]	+	[[Category: Kranzusch, P J]]
-	[[Category: McNamara-Bordewick NK]]	+	[[Category: McNamara-Bordewick, N K]]
-	[[Category: Morehouse BR]]	+	[[Category: Morehouse, B R]]
-	[[Category: Shao S]]	+	[[Category: Shao, S]]
-	[[Category: Yip ~~MCJ~~]]	+	[[Category: Yip, M C.J]]
		+	[[Category: Antiviral protein]]
		+	[[Category: Bacterial]]
		+	[[Category: Filament]]
		+	[[Category: Sting]]

OCA at 18:05, 27 July 2022

OCA — Wed, 27 Jul 2022 18:05:42 GMT

←Older revision		Revision as of 18:05, 27 July 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7un9 is ~~ON HOLD until Paper Publication~~	+	==SfSTING with c-di-GMP double fiber==
-		+	<StructureSection load='7un9' size='340' side='right'caption='[[7un9]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN9 FirstGlance]. <br>
-	~~Description~~:	+	</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=7un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un9 OCA], [https://pdbe.org/7un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un9 RCSB], [https://www.ebi.ac.uk/pdbsum/7un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un9 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Keszei AFA]]
		+	[[Category: Kranzusch PJ]]
		+	[[Category: McNamara-Bordewick NK]]
		+	[[Category: Morehouse BR]]
		+	[[Category: Shao S]]
		+	[[Category: Yip MCJ]]

OCA at 03:50, 8 June 2022

OCA — Wed, 08 Jun 2022 03:50:20 GMT

←Older revision		Revision as of 03:50, 8 June 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7un9 is ON HOLD	+	The entry 7un9 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7un9" [edit=sysop:move=sysop]

OCA — Thu, 21 Apr 2022 01:35:27 GMT

Protected "7un9" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:35, 21 April 2022

OCA: New page: '''Unreleased structure''' The entry 7un9 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Thu, 21 Apr 2022 01:35:26 GMT

New page: '''Unreleased structure''' The entry 7un9 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7un9 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]