6tas: Difference between revisions

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<StructureSection load='6tas' size='340' side='right'caption='[[6tas]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='6tas' size='340' side='right'caption='[[6tas]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6tas]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TAS FirstGlance]. <br>
<table><tr><td colspan='2'>[[6tas]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TAS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Arc1, CG12505 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=6tas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tas OCA], [http://pdbe.org/6tas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tas RCSB], [http://www.ebi.ac.uk/pdbsum/6tas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tas ProSAT]</span></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=6tas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tas OCA], [http://pdbe.org/6tas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tas RCSB], [http://www.ebi.ac.uk/pdbsum/6tas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tas ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ARC1_DROME ARC1_DROME]] Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer from motorneurons to muscles (PubMed:29328915). Arc1 protein is released from motorneurons in extracellular vesicles that mediate the transfer of Arc1 mRNA into muscle cells, where Arc1 mRNA can undergo activity-dependent translation (PubMed:29328915). Intercellular transfer od Arc1 mRNA is required for synaptic plasticity at the neuromuscular junction (PubMed:29328915). May play a role in energy balance: required for regulation of body fat by a specific population of brain neurons, named E347, that are necessary and sufficient for proper body fat storage (PubMed:26209258).<ref>PMID:26209258</ref> <ref>PMID:29328915</ref>   
[[http://www.uniprot.org/uniprot/ARC1_DROME ARC1_DROME]] Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer from motorneurons to muscles (PubMed:29328915). Arc1 protein is released from motorneurons in extracellular vesicles that mediate the transfer of Arc1 mRNA into muscle cells, where Arc1 mRNA can undergo activity-dependent translation (PubMed:29328915). Intercellular transfer od Arc1 mRNA is required for synaptic plasticity at the neuromuscular junction (PubMed:29328915). May play a role in energy balance: required for regulation of body fat by a specific population of brain neurons, named E347, that are necessary and sufficient for proper body fat storage (PubMed:26209258).<ref>PMID:26209258</ref> <ref>PMID:29328915</ref>   
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arc, a neuronal gene that is critical for synaptic plasticity, originated through the domestication of retrotransposon Gag genes and mediates intercellular messenger RNA transfer. We report high-resolution structures of retrovirus-like capsids formed by Drosophila dArc1 and dArc2 that have surface spikes and putative internal RNA-binding domains. These data demonstrate that virus-like capsid-forming properties of Arc are evolutionarily conserved and provide a structural basis for understanding their function in intercellular communication.
Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins.,Erlendsson S, Morado DR, Cullen HB, Feschotte C, Shepherd JD, Briggs JAG Nat Neurosci. 2020 Feb;23(2):172-175. doi: 10.1038/s41593-019-0569-y. Epub 2020, Jan 6. PMID:31907439<ref>PMID:31907439</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tas" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Briggs, J A.G]]
[[Category: Briggs, J A.G]]

Revision as of 10:37, 19 February 2020

Structure of the two-fold capsomer of the dArc1 capsidStructure of the two-fold capsomer of the dArc1 capsid

Structural highlights

6tas is a 8 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:Arc1, CG12505 (DROME)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARC1_DROME] Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer from motorneurons to muscles (PubMed:29328915). Arc1 protein is released from motorneurons in extracellular vesicles that mediate the transfer of Arc1 mRNA into muscle cells, where Arc1 mRNA can undergo activity-dependent translation (PubMed:29328915). Intercellular transfer od Arc1 mRNA is required for synaptic plasticity at the neuromuscular junction (PubMed:29328915). May play a role in energy balance: required for regulation of body fat by a specific population of brain neurons, named E347, that are necessary and sufficient for proper body fat storage (PubMed:26209258).[1] [2]

Publication Abstract from PubMed

Arc, a neuronal gene that is critical for synaptic plasticity, originated through the domestication of retrotransposon Gag genes and mediates intercellular messenger RNA transfer. We report high-resolution structures of retrovirus-like capsids formed by Drosophila dArc1 and dArc2 that have surface spikes and putative internal RNA-binding domains. These data demonstrate that virus-like capsid-forming properties of Arc are evolutionarily conserved and provide a structural basis for understanding their function in intercellular communication.

Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins.,Erlendsson S, Morado DR, Cullen HB, Feschotte C, Shepherd JD, Briggs JAG Nat Neurosci. 2020 Feb;23(2):172-175. doi: 10.1038/s41593-019-0569-y. Epub 2020, Jan 6. PMID:31907439[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Mosher J, Zhang W, Blumhagen RZ, D'Alessandro A, Nemkov T, Hansen KC, Hesselberth JR, Reis T. Coordination between Drosophila Arc1 and a specific population of brain neurons regulates organismal fat. Dev Biol. 2015 Sep 15;405(2):280-90. doi: 10.1016/j.ydbio.2015.07.021. Epub 2015 , Jul 21. PMID:26209258 doi:http://dx.doi.org/10.1016/j.ydbio.2015.07.021
  2. Ashley J, Cordy B, Lucia D, Fradkin LG, Budnik V, Thomson T. Retrovirus-like Gag Protein Arc1 Binds RNA and Traffics across Synaptic Boutons. Cell. 2018 Jan 11;172(1-2):262-274.e11. doi: 10.1016/j.cell.2017.12.022. PMID:29328915 doi:http://dx.doi.org/10.1016/j.cell.2017.12.022
  3. Erlendsson S, Morado DR, Cullen HB, Feschotte C, Shepherd JD, Briggs JAG. Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins. Nat Neurosci. 2020 Feb;23(2):172-175. doi: 10.1038/s41593-019-0569-y. Epub 2020, Jan 6. PMID:31907439 doi:http://dx.doi.org/10.1038/s41593-019-0569-y

6tas, resolution 2.75Å

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OCA