View source for 4ang


==Small RNA phage PRR1 in complex with an RNA operator fragment==
<StructureSection load='4ang' size='340' side='right'caption='[[4ang]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ang]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_PRR1 Pseudomonas phage PRR1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4ang FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ang OCA], [https://pdbe.org/4ang PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ang RCSB], [https://www.ebi.ac.uk/pdbsum/4ang PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ang ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COAT_BPPRR COAT_BPPRR] Forms the phage shell; binds to the phage RNA.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In small RNA bacteriophages, the genomic RNA binds to the coat proteins when the viral capsid assembles. This is achieved through sequence-specific interactions between a coat-protein dimer and an RNA stem-loop that includes the start codon for the replicase gene. The structure of virus-like particles of the small RNA phage PRR1 bound to an RNA segment corresponding to this stem-loop has been solved and the binding was compared with the related, and better investigated, phage MS2. The overall conformation of the RNA is found to be similar and the residues that are involved in RNA binding in PRR1 are the same as in MS2. The arrangement of the nucleotide bases in the loop of the stem-loop is different, leading to a difference in the stacking at the conserved Tyr86, which is equivalent to Tyr85 in MS2.

PRR1 coat protein binding to its RNA translational operator.,Persson M, Tars K, Liljas L Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):367-72. doi:, 10.1107/S0907444912047464. Epub 2013 Feb 16. PMID:23519411<ref>PMID:23519411</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ang" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage PRR1]]
[[Category: Liljas L]]
[[Category: Persson M]]
[[Category: Tars K]]