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 </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bml RCSB], [http://www.ebi.ac.uk/pdbsum/4bml PDBsum]</span></td></tr>
 <table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Marine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-A structure of a cyanobacterial virus, Syn5, by electron cryo-microscopy and modelling. A Calpha backbone trace of the major capsid protein (gp39) reveals a classic phage protein fold. In addition, two knob-like proteins protruding from the capsid surface are also observed. Using bioinformatics and structure analysis tools, these proteins are identified to correspond to gp55 and gp58 (each with two copies per asymmetric unit). The non 1:1 stoichiometric distribution of gp55/58 to gp39 breaks all expected local symmetries and leads to non-quasi-equivalence of the capsid subunits, suggesting a role in capsid stabilization. Such a structural arrangement has not yet been observed in any known virus structures.
+Protruding knob-like proteins violate local symmetries in an icosahedral marine virus.,Gipson P, Baker ML, Raytcheva D, Haase-Pettingell C, Piret J, King JA, Chiu W Nat Commun. 2014 Jul 2;5:4278. doi: 10.1038/ncomms5278. PMID:24985522<ref>PMID:24985522</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>