7nli

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Current revision (11:14, 23 October 2024) (edit) (undo)
 
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<StructureSection load='7nli' size='340' side='right'caption='[[7nli]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
<StructureSection load='7nli' size='340' side='right'caption='[[7nli]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7nli]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NLI FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NLI 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]] 3.119&#8491;</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]] 3.119&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7nli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nli OCA], [https://pdbe.org/7nli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nli RCSB], [https://www.ebi.ac.uk/pdbsum/7nli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nli 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=7nli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nli OCA], [https://pdbe.org/7nli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nli RCSB], [https://www.ebi.ac.uk/pdbsum/7nli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nli ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/TY1A_YEASX TY1A_YEASX] Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription.<ref>PMID:10766747</ref>
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== Publication Abstract from PubMed ==
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Excessive replication of Saccharomyces cerevisiae Ty1 retrotransposons is regulated by Copy Number Control, a process requiring the p22/p18 protein produced from a sub-genomic transcript initiated within Ty1 GAG. In retrotransposition, Gag performs the capsid functions required for replication and re-integration. To minimize genomic damage, p22/p18 interrupts virus-like particle function by interaction with Gag. Here, we present structural, biophysical and genetic analyses of p18m, a minimal fragment of Gag that restricts transposition. The 2.8 A crystal structure of p18m reveals an all alpha-helical protein related to mammalian and insect ARC proteins. p18m retains the capacity to dimerise in solution and the crystal structures reveal two exclusive dimer interfaces. We probe our findings through biophysical analysis of interface mutants as well as Ty1 transposition and p18m restriction in vivo. Our data provide insight into Ty1 Gag structure and suggest how p22/p18 might function in restriction through a blocking-of-assembly mechanism.
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Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.,Cottee MA, Beckwith SL, Letham SC, Kim SJ, Young GR, Stoye JP, Garfinkel DJ, Taylor IA Nat Commun. 2021 Sep 22;12(1):5590. doi: 10.1038/s41467-021-25849-0. PMID:34552077<ref>PMID:34552077</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7nli" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
 
[[Category: Cottee MA]]
[[Category: Cottee MA]]
[[Category: Letham SC]]
[[Category: Letham SC]]
[[Category: Taylor IA]]
[[Category: Taylor IA]]

Current revision

S. cerevisiae Ty1 p22 restriction factor, Gag CA-CTD, AUG2 variant

PDB ID 7nli

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