View source for 8fmh


==Structure of CBASS Cap5 from Pseudomonas syringae as an activated tetramer with the cyclic dinucleotide 3'2'-c-dGAMP ligand (2 tetramers in the AU)==
<StructureSection load='8fmh' size='340' side='right'caption='[[8fmh]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fmh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FMH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4UR:32-CGAMP'>4UR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8fmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fmh OCA], [https://pdbe.org/8fmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fmh RCSB], [https://www.ebi.ac.uk/pdbsum/8fmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fmh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2P0QGK5_PSESF A0A2P0QGK5_PSESF] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial cyclic oligonucleotide-based antiphage signaling system (CBASS) is similar to the cGAS-STING system in humans, containing an enzyme that synthesizes a cyclic nucleotide on viral infection and an effector that senses the second messenger for the antiviral response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease domain, is the most abundant CBASS effector, yet the mechanism by which it becomes activated for cell killing remains unknown. We present here high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) with second messengers. The key to PsCap5 activation is a dimer-to-tetramer transition, whereby the binding of second messenger to dimer triggers an open-to-closed transformation of the SAVED domains, furnishing a surface for assembly of the tetramer. This movement propagates to the HNH domains, juxtaposing and converting two HNH domains into states for DNA destruction. These results show how Cap5 effects bacterial cell suicide and we provide proof-in-principle data that the CBASS can be extrinsically activated to limit bacterial infections.

Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides.,Rechkoblit O, Sciaky D, Kreitler DF, Buku A, Kottur J, Aggarwal AK Nat Struct Mol Biol. 2024 May;31(5):767-776. doi: 10.1038/s41594-024-01220-x. , Epub 2024 Feb 6. PMID:38321146<ref>PMID:38321146</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8fmh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas syringae]]
[[Category: Aggarwal AK]]
[[Category: Kreitler DF]]
[[Category: Rechkoblit O]]