8fex: Difference between revisions

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'''Unreleased structure'''


The entry 8fex is ON HOLD
==Inactivate state of Maribacter polysiphoniae Argonuate (short pAgo system)==
<StructureSection load='8fex' size='340' side='right'caption='[[8fex]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Maribacter_polysiphoniae Maribacter polysiphoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FEX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.07&#8491;</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=8fex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fex OCA], [https://pdbe.org/8fex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fex RCSB], [https://www.ebi.ac.uk/pdbsum/8fex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fex ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A316E683_9FLAO A0A316E683_9FLAO]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although eukaryotic and long prokaryotic Argonaute proteins (pAgos) cleave nucleic acids, some short pAgos lack nuclease activity and hydrolyse NAD(P)(+) to induce bacterial cell death(1). Here we present a hierarchical activation pathway for SPARTA, a short pAgo consisting of an Argonaute (Ago) protein and TIR-APAZ, an associated protein(2). SPARTA progresses through distinct oligomeric forms, including a monomeric apo state, a monomeric RNA-DNA-bound state, two dimeric RNA-DNA-bound states and a tetrameric RNA-DNA-bound active state. These snapshots together identify oligomerization as a mechanistic principle of SPARTA activation. The RNA-DNA-binding channel of apo inactive SPARTA is occupied by an auto-inhibitory motif in TIR-APAZ. After the binding of RNA-DNA, SPARTA transitions from a monomer to a symmetric dimer and then an asymmetric dimer, in which two TIR domains interact through charge and shape complementarity. Next, two dimers assemble into a tetramer with a central TIR cluster responsible for hydrolysing NAD(P)(+). In addition, we observe unique features of interactions between SPARTA and RNA-DNA, including competition between the DNA 3' end and the auto-inhibitory motif, interactions between the RNA G2 nucleotide and Ago, and splaying of the RNA-DNA duplex by two loops exclusive to short pAgos. Together, our findings provide a mechanistic basis for the activation of short pAgos, a large section of the Ago superfamily.


Authors:  
Oligomerization-mediated activation of a short prokaryotic Argonaute.,Shen Z, Yang XY, Xia S, Huang W, Taylor DJ, Nakanishi K, Fu TM Nature. 2023 Sep;621(7977):154-161. doi: 10.1038/s41586-023-06456-z. Epub 2023 , Jul 26. PMID:37494956<ref>PMID:37494956</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8fex" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Maribacter polysiphoniae]]
[[Category: Fu TM]]
[[Category: Shen ZF]]
[[Category: Yang XY]]
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