6wan

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'''Unreleased structure'''
 
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The entry 6wan is ON HOLD until Paper Publication
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==Structure of Acinetobacter baumannii Cap4 SAVED/CARF-domain containing receptor with the cyclic trinucleotide 3'3'3'-cAAA==
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<StructureSection load='6wan' size='340' side='right'caption='[[6wan]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6wan]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WAN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=SO4:SULFATE+ION'>SO4</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=6wan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wan OCA], [https://pdbe.org/6wan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wan RCSB], [https://www.ebi.ac.uk/pdbsum/6wan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wan ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAP4_ACIS2 CAP4_ACIS2] 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 II-C(AAAA) CBASS system (PubMed:32839535).<ref>PMID:32839535</ref> <ref>PMID:32544385</ref> Binds cyclic nucleotide second messengers (synthesized by CdnD, the cognate CD-NTase in the CBASS operon). Ligand binding activates it to endonucleolytically degrade dsDNA to approximately 6 bp length fragments, with a preference for 5'-C or 5'-G cleavage site. The minor product of CdnD is the activating nucleotide; also binds the major product (2',3',3'-cyclic AMP-AMP-AMP) but is not activated by it. Only binds DNA in the presence of ligand. Is not activated by c-di-AMP, c-di-GMP, 3'3'-cyclic GMP-AMP (3'3'-cGAMP) or 3',3',3'-cyclic AMP-AMP-GMP.<ref>PMID:32544385</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzymes are immune sensors that synthesize nucleotide second messengers and initiate antiviral responses in bacterial and animal cells. Here, we discover Enterobacter cloacae CD-NTase-associated protein 4 (Cap4) as a founding member of a diverse family of &gt;2,000 bacterial receptors that respond to CD-NTase signals. Structures of Cap4 reveal a promiscuous DNA endonuclease domain activated through ligand-induced oligomerization. Oligonucleotide recognition occurs through an appended SAVED domain that is an unexpected fusion of two CRISPR-associated Rossman fold (CARF) subunits co-opted from type III CRISPR immunity. Like a lock and key, SAVED effectors exquisitely discriminate 2'-5'- and 3'-5'-linked bacterial cyclic oligonucleotide signals and enable specific recognition of at least 180 potential nucleotide second messenger species. Our results reveal SAVED CARF family proteins as major nucleotide second messenger receptors in CBASS and CRISPR immune defense and extend the importance of linkage specificity beyond mammalian cGAS-STING signaling.
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Authors:
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CBASS Immunity Uses CARF-Related Effectors to Sense 3'-5'- and 2'-5'-Linked Cyclic Oligonucleotide Signals and Protect Bacteria from Phage Infection.,Lowey B, Whiteley AT, Keszei AFA, Morehouse BR, Mathews IT, Antine SP, Cabrera VJ, Kashin D, Niemann P, Jain M, Schwede F, Mekalanos JJ, Shao S, Lee ASY, Kranzusch PJ Cell. 2020 Jun 4. pii: S0092-8674(20)30614-0. doi: 10.1016/j.cell.2020.05.019. PMID:32544385<ref>PMID:32544385</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6wan" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Acinetobacter baumannii]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Antine SP]]
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[[Category: Cabrera V]]
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[[Category: Keszei AFA]]
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[[Category: Kranzusch PJ]]
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[[Category: Lee ASY]]
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[[Category: Lowey B]]
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[[Category: Mekalanos JJ]]
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[[Category: Morehouse BR]]
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[[Category: Schwede F]]
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[[Category: Shao S]]
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[[Category: Whiteley AT]]

Current revision

Structure of Acinetobacter baumannii Cap4 SAVED/CARF-domain containing receptor with the cyclic trinucleotide 3'3'3'-cAAA

PDB ID 6wan

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