5n95: Difference between revisions
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==Tetragonal structure of mutant V173I of 3D polymerase from Foot-and-Mouth Disease Virus== | |||
<StructureSection load='5n95' size='340' side='right' caption='[[5n95]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n95]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N95 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N95 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n95 OCA], [http://pdbe.org/5n95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n95 RCSB], [http://www.ebi.ac.uk/pdbsum/5n95 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n95 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The selective pressures acting on viruses that replicate under enhanced mutation rates are largely unknown. Here we describe resistance of foot-and-mouth disease virus (FMDV) to the mutagen 5-fluorouracil (FU) through a single polymerase substitution that prevents an excess of A to G and U to C transitions evoked by FU on the wild-type FMDV, while maintaining the same level of mutant spectrum complexity. The polymerase substitution inflicts upon the virus a fitness loss during replication in absence of FU but confers a fitness gain in presence of FU. The compensation of mutational bias was documented by in vitro nucleotide incorporation assays, and it was associated with structural modifications at the N-terminal region and motif B of the viral polymerase. Predictions of the effect of mutations that increase the frequency of G and C in the viral genome and encoded polymerase suggest multiple points in the virus life cycle where the mutational bias in favor of G and C may be detrimental. Application of predictive algorithms suggest adverse effects of the FU-directed mutational bias on protein stability. The results reinforce modulation of nucleotide incorporation as a lethal mutagenesis-escape mechanism (that permits eluding virus extinction despite replication in the presence of a mutagenic agent) and suggest that mutational bias can be a target of selection during virus replication. | |||
Molecular and functional bases of selection against a mutation bias in an RNA virus.,de la Higuera I, Ferrer-Orta C, de Avila AI, Perales C, Sierra M, Singh K, Sarafianos SG, Dehouck Y, Bastolla U, Verdaguer N, Domingo E Genome Biol Evol. 2017 Apr 27. doi: 10.1093/gbe/evx075. PMID:28460010<ref>PMID:28460010</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5n95" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ferrer-Orta, C]] | |||
[[Category: Verdaguer, N]] | [[Category: Verdaguer, N]] | ||
[[Category: | [[Category: 5'-fluoracil]] | ||
[[Category: Nucleotide analogue]] | |||
[[Category: Rna dependent rna polymerase]] | |||
[[Category: Viral protein]] | |||
