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| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4dq7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQ7 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4dq7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQ7 FirstGlance]. <br> |
| </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=4dq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dq7 OCA], [https://pdbe.org/4dq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dq7 RCSB], [https://www.ebi.ac.uk/pdbsum/4dq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dq7 ProSAT]</span></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</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=4dq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dq7 OCA], [https://pdbe.org/4dq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dq7 RCSB], [https://www.ebi.ac.uk/pdbsum/4dq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dq7 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/Q283U5_BPPH6 Q283U5_BPPH6]]
| | [https://www.uniprot.org/uniprot/Q283U5_BPPH6 Q283U5_BPPH6] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| The modulation of fitness by single mutational substitutions during environmental change is the most fundamental consequence of natural selection. The antagonistic tradeoffs of pleiotropic mutations that can be selected under changing environments therefore lie at the foundation of evolutionary biology. However, the molecular basis of fitness tradeoffs is rarely determined in terms of how these pleiotropic mutations affect protein structure. Here we use an interdisciplinary approach to study how antagonistic pleiotropy and protein function dictate a fitness tradeoff. We challenged populations of an RNA virus, bacteriophage Phi6, to evolve in a novel temperature environment where heat shock imposed extreme virus mortality. A single amino acid substitution in the viral lysin protein P5 (V207F) favored improved stability, and hence survival of challenged viruses, despite a concomitant tradeoff that decreased viral reproduction. This mutation increased the thermostability of P5. Crystal structures of wild-type, mutant, and ligand-bound P5 reveal the molecular basis of this thermostabilization--the Phe207 side chain fills a hydrophobic cavity that is unoccupied in the wild-type--and identify P5 as a lytic transglycosylase. The mutation did not reduce the enzymatic activity of P5, suggesting that the reproduction tradeoff stems from other factors such as inefficient capsid assembly or disassembly. Our study demonstrates how combining experimental evolution, biochemistry, and structural biology can identify the mechanisms that drive the antagonistic pleiotropic phenotypes of an individual point mutation in the classic evolutionary tug-of-war between survival and reproduction.
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| Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme.,Dessau M, Goldhill D, McBride R, Turner PE, Modis Y PLoS Genet. 2012;8(11):e1003102. doi: 10.1371/journal.pgen.1003102. Epub 2012 Nov, 29. PMID:23209446<ref>PMID:23209446</ref>
| | ==See Also== |
| | | *[[Lysin 3D structures|Lysin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4dq7" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |