4bcu: Difference between revisions
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The | ==Satellite Tobacco Necrosis Virus (STNV) virus like particle in complex with the B3 aptamer== | ||
<StructureSection load='4bcu' size='340' side='right'caption='[[4bcu]], [[Resolution|resolution]] 2.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bcu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Satellite_tobacco_mosaic_virus Satellite tobacco mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BCU 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]] 2.29Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=4bcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bcu OCA], [https://pdbe.org/4bcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bcu RCSB], [https://www.ebi.ac.uk/pdbsum/4bcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bcu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAPSD_STNV1 CAPSD_STNV1] Self-assembles to form an icosahedral capsid of 17 nm in diameter.<ref>PMID:21839089</ref> <ref>PMID:23318955</ref> <ref>PMID:6481804</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have examined the roles of RNA-coat protein (CP) interactions in the assembly of satellite tobacco necrosis virus (STNV). The viral genomic RNA encodes only the CP, which comprises a beta-barrel domain connected to a positively charged N-terminal extension. In the previous crystal structures of this system, the first 11 residues of the protein are disordered. Using variants of an RNA aptamer sequence isolated against the CP, B3, we have studied the sequence specificity of RNA-induced assembly. B3 consists of a stem-loop presenting the tetra-loop sequence ACAA. There is a clear preference for RNAs encompassing this loop sequence, as measured by the yield of T=1 capsids, which is indifferent to sequences within the stem. The B3-containing virus-like particle has been crystallised and its structure was determined to 2.3A. A lower-resolution map encompassing density for the RNA has also been calculated. The presence of B3 results in increased ordering of the N-terminal helices located at the particle 3-fold axes, which extend by roughly one and a half turns to encompass residues 8-11, including R8 and K9. Under assembly conditions, STNV CP in the absence of RNA is monomeric and does not self-assemble. These facts suggest that a plausible model for assembly initiation is the specific RNA-induced stabilisation of a trimeric capsomere. The basic nature of the helical extension suggests that electrostatic repulsion between CPs prevents assembly in the absence of RNA and that this barrier is overcome by correct placement of appropriately orientated helical RNA stems. Such a mechanism would be consistent with the data shown here for assembly with longer RNA fragments, including an STNV genome. The results are discussed in light of a first stage of assembly involving compaction of the genomic RNA driven by multiple RNA packaging signal-CP interactions. | |||
Sequence-Specific, RNA-Protein Interactions Overcome Electrostatic Barriers Preventing Assembly of Satellite Tobacco Necrosis Virus Coat Protein.,Ford RJ, Barker AM, Bakker SE, Coutts RH, Ranson NA, Phillips SE, Pearson AR, Stockley PG J Mol Biol. 2013 Jan 11. pii: S0022-2836(13)00007-7. doi:, 10.1016/j.jmb.2013.01.004. PMID:23318955<ref>PMID:23318955</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bcu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tobacco Mosaic Virus|Tobacco Mosaic Virus]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Satellite tobacco mosaic virus]] | |||
[[Category: Bakker SE]] | |||
[[Category: Barker AM]] | |||
[[Category: Coutts RH]] | |||
[[Category: Ford RJ]] | |||
[[Category: Pearson AR]] | |||
[[Category: Phillips SEV]] | |||
[[Category: Ranson NA]] | |||
[[Category: Stockley PG]] | |||
Latest revision as of 13:59, 9 May 2024
Satellite Tobacco Necrosis Virus (STNV) virus like particle in complex with the B3 aptamerSatellite Tobacco Necrosis Virus (STNV) virus like particle in complex with the B3 aptamer
Structural highlights
FunctionCAPSD_STNV1 Self-assembles to form an icosahedral capsid of 17 nm in diameter.[1] [2] [3] Publication Abstract from PubMedWe have examined the roles of RNA-coat protein (CP) interactions in the assembly of satellite tobacco necrosis virus (STNV). The viral genomic RNA encodes only the CP, which comprises a beta-barrel domain connected to a positively charged N-terminal extension. In the previous crystal structures of this system, the first 11 residues of the protein are disordered. Using variants of an RNA aptamer sequence isolated against the CP, B3, we have studied the sequence specificity of RNA-induced assembly. B3 consists of a stem-loop presenting the tetra-loop sequence ACAA. There is a clear preference for RNAs encompassing this loop sequence, as measured by the yield of T=1 capsids, which is indifferent to sequences within the stem. The B3-containing virus-like particle has been crystallised and its structure was determined to 2.3A. A lower-resolution map encompassing density for the RNA has also been calculated. The presence of B3 results in increased ordering of the N-terminal helices located at the particle 3-fold axes, which extend by roughly one and a half turns to encompass residues 8-11, including R8 and K9. Under assembly conditions, STNV CP in the absence of RNA is monomeric and does not self-assemble. These facts suggest that a plausible model for assembly initiation is the specific RNA-induced stabilisation of a trimeric capsomere. The basic nature of the helical extension suggests that electrostatic repulsion between CPs prevents assembly in the absence of RNA and that this barrier is overcome by correct placement of appropriately orientated helical RNA stems. Such a mechanism would be consistent with the data shown here for assembly with longer RNA fragments, including an STNV genome. The results are discussed in light of a first stage of assembly involving compaction of the genomic RNA driven by multiple RNA packaging signal-CP interactions. Sequence-Specific, RNA-Protein Interactions Overcome Electrostatic Barriers Preventing Assembly of Satellite Tobacco Necrosis Virus Coat Protein.,Ford RJ, Barker AM, Bakker SE, Coutts RH, Ranson NA, Phillips SE, Pearson AR, Stockley PG J Mol Biol. 2013 Jan 11. pii: S0022-2836(13)00007-7. doi:, 10.1016/j.jmb.2013.01.004. PMID:23318955[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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