2vf9: Difference between revisions
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< | ==Crystal structure of bacteriophage PRR1== | ||
<StructureSection load='2vf9' size='340' side='right'caption='[[2vf9]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vf9]] is a 3 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=2VF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VF9 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]] 3.5Å</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=2vf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vf9 OCA], [https://pdbe.org/2vf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vf9 RCSB], [https://www.ebi.ac.uk/pdbsum/2vf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vf9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/COAT_BPPRR COAT_BPPRR] Forms the phage shell; binds to the phage RNA. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vf/2vf9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vf9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many nonenveloped virus particles are stabilized by calcium ions bound in the interfaces between the protein subunits. These ions may have a role in the disassembly process. The small RNA phages of the Leviviridae family have T=3 quasi-symmetry and are unique among simple viruses in that they have a coat protein with a translational repressor activity and a fold that has not been observed in other viruses. The crystal structure of phage PRR1 has been determined to 3.5 A resolution. The structure shows a tentative binding site for a calcium ion close to the quasi-3-fold axis. The RNA-binding surface used for repressor activity is mostly conserved. The structure does not show any significant differences between quasi-equivalent subunits, which suggests that the assembly is not controlled by conformational switches as in many other simple viruses. | |||
The capsid of the small RNA phage PRR1 is stabilized by metal ions.,Persson M, Tars K, Liljas L J Mol Biol. 2008 Nov 21;383(4):914-22. Epub 2008 Aug 29. PMID:18786545<ref>PMID:18786545</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2vf9" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Liljas | __TOC__ | ||
[[Category: Persson | </StructureSection> | ||
[[Category: Tars | [[Category: Large Structures]] | ||
[[Category: Pseudomonas phage PRR1]] | |||
[[Category: Liljas L]] | |||
[[Category: Persson M]] | |||
[[Category: Tars K]] | |||