View source for 7a4j


==Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-4==
<StructureSection load='7a4j' size='340' side='right'caption='[[7a4j]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7a4j]] is a 240 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A4J FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ribH, aq_132 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</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=7a4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a4j OCA], [https://pdbe.org/7a4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a4j RCSB], [https://www.ebi.ac.uk/pdbsum/7a4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a4j ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/REGN_LAMBD REGN_LAMBD]] Antitermination proteins positively regulate expression of the phage early and late gene operons. Bacterial host RNA polymerase modified by these antitermination proteins transcribes through termination sites that otherwise prevent expression of the regulated genes.  N protein regulates the transition from the early to the middle stage of lytic development. It is a transcription antitermination protein that prevents termination at the rho-dependent tL and tR transcription termination sites. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viruses are ubiquitous pathogens of global impact. Prompted by the hypothesis that their earliest progenitors recruited host proteins for virion formation, we have used stringent laboratory evolution to convert a bacterial enzyme that lacks affinity for nucleic acids into an artificial nucleocapsid that efficiently packages and protects multiple copies of its own encoding messenger RNA. Revealing remarkable convergence on the molecular hallmarks of natural viruses, the accompanying changes reorganized the protein building blocks into an interlaced 240-subunit icosahedral capsid that is impermeable to nucleases, and emergence of a robust RNA stem-loop packaging cassette ensured high encapsidation yields and specificity. In addition to evincing a plausible evolutionary pathway for primordial viruses, these findings highlight practical strategies for developing nonviral carriers for diverse vaccine and delivery applications.

Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein.,Tetter S, Terasaka N, Steinauer A, Bingham RJ, Clark S, Scott AJP, Patel N, Leibundgut M, Wroblewski E, Ban N, Stockley PG, Twarock R, Hilvert D Science. 2021 Jun 11;372(6547):1220-1224. doi: 10.1126/science.abg2822. PMID:34112695<ref>PMID:34112695</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7a4j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteriophage lambda]]
[[Category: Large Structures]]
[[Category: Hilvert, D]]
[[Category: Tetter, S]]
[[Category: Capsid]]
[[Category: Design]]
[[Category: Virus like particle]]
[[Category: Virus mimic]]