5tc1: Difference between revisions

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<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ms2|2ms2]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 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=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [https://pdbe.org/5tc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [https://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref> 
[https://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Packaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host 'sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 A resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3' end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded beta-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses.
 
In situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus.,Dai X, Li Z, Lai M, Shu S, Du Y, Zhou ZH, Sun R Nature. 2017 Jan 5;541(7635):112-116. doi: 10.1038/nature20589. Epub 2016 Dec 19. PMID:27992877<ref>PMID:27992877</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</SX>
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[[Category: Enterobacteria phage ms2]]
[[Category: Escherichia virus MS2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dai, X H]]
[[Category: Dai XH]]
[[Category: Du, Y S]]
[[Category: Du YS]]
[[Category: Lai, M]]
[[Category: Lai M]]
[[Category: Li, Z H]]
[[Category: Li ZH]]
[[Category: Shu, S]]
[[Category: Shu S]]
[[Category: Sun, R]]
[[Category: Sun R]]
[[Category: Zhou, Z H]]
[[Category: Zhou ZH]]
[[Category: Asymmetric cryoem reconstruction]]
[[Category: Genome-capsid interaction]]
[[Category: Genome-delivery apparatus]]
[[Category: Ssrna genome structure]]
[[Category: Viral protein-rna complex]]
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