6p8p: Difference between revisions

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<StructureSection load='6p8p' size='340' side='right'caption='[[6p8p]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
<StructureSection load='6p8p' size='340' side='right'caption='[[6p8p]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6p8p]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P8P FirstGlance]. <br>
<table><tr><td colspan='2'>[[6p8p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P8P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 1.635&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DY979_07575, EGY23_20885, IPC669_24870, PA5486_02900, PAERUG_E15_London_28_01_14_04349 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6p8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p8p OCA], [http://pdbe.org/6p8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p8p RCSB], [http://www.ebi.ac.uk/pdbsum/6p8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p8p 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=6p8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p8p OCA], [https://pdbe.org/6p8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p8p RCSB], [https://www.ebi.ac.uk/pdbsum/6p8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p8p ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/CAP8_PSEAI CAP8_PSEAI] 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 III-C(AAA) CBASS system (PubMed:32839535).<ref>PMID:31932165</ref> <ref>PMID:32839535</ref>   A member of the CBASS system in this bacteria. It does not seem to bind a closure peptide, its exact function is unknown.<ref>PMID:31932165</ref>  
Bacteria are continually challenged by foreign invaders, including bacteriophages, and have evolved a variety of defenses against these invaders. Here, we describe the structural and biochemical mechanisms of a bacteriophage immunity pathway found in a broad array of bacteria, including E. coli and Pseudomonas aeruginosa. This pathway uses eukaryotic-like HORMA domain proteins that recognize specific peptides, then bind and activate a cGAS/DncV-like nucleotidyltransferase (CD-NTase) to generate a cyclic triadenylate (cAAA) second messenger; cAAA in turn activates an endonuclease effector, NucC. Signaling is attenuated by a homolog of the AAA+ ATPase Pch2/TRIP13, which binds and disassembles the active HORMA-CD-NTase complex. When expressed in non-pathogenic E. coli, this pathway confers immunity against bacteriophage lambda through an abortive infection mechanism. Our findings reveal the molecular mechanisms of a bacterial defense pathway integrating a cGAS-like nucleotidyltransferase with HORMA domain proteins for threat sensing through protein detection and negative regulation by a Trip13 ATPase.
 
HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-like Enzymes to Mediate Bacteriophage Immunity.,Ye Q, Lau RK, Mathews IT, Birkholz EA, Watrous JD, Azimi CS, Pogliano J, Jain M, Corbett KD Mol Cell. 2019 Dec 31. pii: S1097-2765(19)30922-0. doi:, 10.1016/j.molcel.2019.12.009. PMID:31932165<ref>PMID:31932165</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6p8p" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Corbett, K D]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Ye, Q]]
[[Category: Corbett KD]]
[[Category: Cd-ntase]]
[[Category: Ye Q]]
[[Category: Horma domain]]
[[Category: Protein binding]]

Latest revision as of 14:54, 13 March 2024

Structure of P. aeruginosa ATCC27853 HORMA1

6p8p, resolution 1.64Å

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