6yfd: Difference between revisions
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==Virus-like particle of Beihai levi-like virus 14== | ==Virus-like particle of Beihai levi-like virus 14== | ||
<StructureSection load='6yfd' size='340' side='right'caption='[[6yfd]]' scene=''> | <StructureSection load='6yfd' size='340' side='right'caption='[[6yfd]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YFD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YFD FirstGlance]. <br> | <table><tr><td colspan='2'>[[6yfd]] is a 90 chain structure with sequence from [http://en.wikipedia.org/wiki/Beihai_levi-like_virus_14 Beihai levi-like virus 14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YFD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YFD FirstGlance]. <br> | ||
</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=6yfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yfd OCA], [http://pdbe.org/6yfd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yfd RCSB], [http://www.ebi.ac.uk/pdbsum/6yfd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yfd ProSAT]</span></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6yf7|6yf7]], [[6yf9|6yf9]], [[6yfa|6yfa]], [[6yfb|6yfb]], [[6yfc|6yfc]], [[6yfe|6yfe]], [[6yff|6yff]], [[6yfg|6yfg]], [[6yfh|6yfh]], [[6yfi|6yfi]], [[6yfj|6yfj]], [[6yfk|6yfk]], [[6yfl|6yfl]], [[6yfm|6yfm]], [[6yfn|6yfn]], [[6yfo|6yfo]], [[6yfp|6yfp]], [[6yfq|6yfq]], [[6yfr|6yfr]], [[6yfs|6yfs]], [[6yft|6yft]], [[6yfu|6yfu]]</div></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=6yfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yfd OCA], [http://pdbe.org/6yfd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yfd RCSB], [http://www.ebi.ac.uk/pdbsum/6yfd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yfd ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The single-stranded RNA (ssRNA) bacteriophages are among the simplest known viruses with small genomes and exceptionally high mutation rates. The number of ssRNA phage isolates has remained very low, but recent metagenomic studies have uncovered an immense variety of distinct uncultured ssRNA phages. The coat proteins (CPs) in these genomes are particularly diverse, with notable variation in length and often no recognizable similarity to previously known viruses. We recombinantly expressed metagenome-derived ssRNA phage CPs to produce virus-like particles and determined the three-dimensional structure of 22 previously uncharacterized ssRNA phage capsids covering nine distinct CP types. The structures revealed substantial deviations from the previously known ssRNA phage CP fold, uncovered an unusual prolate particle shape, and revealed a previously unseen dsRNA binding mode. These data expand our knowledge of the evolution of viral structural proteins and are of relevance for applications such as ssRNA phage-based vaccine design. | |||
Three-dimensional structure of 22 uncultured ssRNA bacteriophages: Flexibility of the coat protein fold and variations in particle shapes.,Rumnieks J, Lieknina I, Kalnins G, Sisovs M, Akopjana I, Bogans J, Tars K Sci Adv. 2020 Sep 2;6(36). pii: 6/36/eabc0023. doi: 10.1126/sciadv.abc0023. Print, 2020 Sep. PMID:32917600<ref>PMID:32917600</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6yfd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beihai levi-like virus 14]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kalnins G]] | [[Category: Kalnins, G]] | ||
[[Category: Lieknina I]] | [[Category: Lieknina, I]] | ||
[[Category: Rumnieks J]] | [[Category: Rumnieks, J]] | ||
[[Category: Sisovs M]] | [[Category: Sisovs, M]] | ||
[[Category: Tars K]] | [[Category: Tars, K]] | ||
[[Category: Structural protein]] | |||
[[Category: Virus]] | |||
[[Category: Virus like particle]] | |||
[[Category: Virus-like particle]] | |||
Revision as of 15:54, 16 December 2020
Virus-like particle of Beihai levi-like virus 14Virus-like particle of Beihai levi-like virus 14
Structural highlights
Publication Abstract from PubMedThe single-stranded RNA (ssRNA) bacteriophages are among the simplest known viruses with small genomes and exceptionally high mutation rates. The number of ssRNA phage isolates has remained very low, but recent metagenomic studies have uncovered an immense variety of distinct uncultured ssRNA phages. The coat proteins (CPs) in these genomes are particularly diverse, with notable variation in length and often no recognizable similarity to previously known viruses. We recombinantly expressed metagenome-derived ssRNA phage CPs to produce virus-like particles and determined the three-dimensional structure of 22 previously uncharacterized ssRNA phage capsids covering nine distinct CP types. The structures revealed substantial deviations from the previously known ssRNA phage CP fold, uncovered an unusual prolate particle shape, and revealed a previously unseen dsRNA binding mode. These data expand our knowledge of the evolution of viral structural proteins and are of relevance for applications such as ssRNA phage-based vaccine design. Three-dimensional structure of 22 uncultured ssRNA bacteriophages: Flexibility of the coat protein fold and variations in particle shapes.,Rumnieks J, Lieknina I, Kalnins G, Sisovs M, Akopjana I, Bogans J, Tars K Sci Adv. 2020 Sep 2;6(36). pii: 6/36/eabc0023. doi: 10.1126/sciadv.abc0023. Print, 2020 Sep. PMID:32917600[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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