View source for 5oac


==FLiP major capsid protein==
<SX load='5oac' size='340' side='right' viewer='molstar' caption='[[5oac]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oac]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_sp. Bacteriophage sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OAC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</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=5oac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oac OCA], [https://pdbe.org/5oac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oac RCSB], [https://www.ebi.ac.uk/pdbsum/5oac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oac ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2D0TC94_9VIRU A0A2D0TC94_9VIRU] 
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== Publication Abstract from PubMed ==
Viruses have impacted the biosphere in numerous ways since the dawn of life. However, the evolution, genetic, structural, and taxonomic diversity of viruses remain poorly understood, in part because sparse sampling of the virosphere has concentrated mostly on exploring the abundance and diversity of dsDNA viruses. Furthermore, viral genomes are highly diverse, and using only the current sequence-based methods for classifying viruses and studying their phylogeny is complicated. Here we describe a virus, FLiP (Flavobacterium-infecting, lipid-containing phage), with a circular ssDNA genome and an internal lipid membrane enclosed in the icosahedral capsid. The 9,174-nt-long genome showed limited sequence similarity to other known viruses. The genetic data imply that this virus might use replication mechanisms similar to those found in other ssDNA replicons. However, the structure of the viral major capsid protein, elucidated at near-atomic resolution using cryo-electron microscopy, is strikingly similar to that observed in dsDNA viruses of the PRD1-adenovirus lineage, characterized by a major capsid protein bearing two beta-barrels. The strong similarity between FLiP and another member of the structural lineage, bacteriophage PM2, extends to the capsid organization (pseudo T = 21 dextro) despite the difference in the genetic material packaged and the lack of significant sequence similarity.

Virus found in a boreal lake links ssDNA and dsDNA viruses.,Laanto E, Mantynen S, De Colibus L, Marjakangas J, Gillum A, Stuart DI, Ravantti JJ, Huiskonen JT, Sundberg LR Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):8378-8383. doi:, 10.1073/pnas.1703834114. Epub 2017 Jul 17. PMID:28716906<ref>PMID:28716906</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5oac" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Bacteriophage sp]]
[[Category: Large Structures]]
[[Category: De Colibus L]]
[[Category: Huiskonen JT]]
[[Category: Stuart DI]]