2qqp: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Crystal Structure of Authentic Providence Virus== | ==Crystal Structure of Authentic Providence Virus== | ||
<StructureSection load='2qqp' size='340' side='right' caption='[[2qqp]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='2qqp' size='340' side='right' caption='[[2qqp]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[2qqp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Providence_virus Providence virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QQP FirstGlance]. <br> | <table><tr><td colspan='2'>[[2qqp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Providence_virus Providence virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QQP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqp OCA], [http://pdbe.org/2qqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqp RCSB], [http://www.ebi.ac.uk/pdbsum/2qqp PDBsum]</span></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=2qqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqp OCA], [http://pdbe.org/2qqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqp RCSB], [http://www.ebi.ac.uk/pdbsum/2qqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Line 14: | Line 15: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2qqp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Line 25: | Line 26: | ||
</div> | </div> | ||
<div class="pdbe-citations 2qqp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2qqp" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:33, 25 October 2017
Crystal Structure of Authentic Providence VirusCrystal Structure of Authentic Providence Virus
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe T = 4 tetravirus and T = 3 nodavirus capsid proteins undergo closely similar autoproteolysis to produce the N-terminal beta and C-terminal, lipophilic gamma polypeptides. The gamma peptides and the N termini of beta also act as molecular switches that determine their quasi equivalent capsid structures. The crystal structure of Providence virus (PrV), only the second of a tetravirus (the first was NomegaV), reveals conserved folds and cleavage sites, but the protein termini have completely different structures and the opposite functions of those in NomegaV. N termini of beta form the molecular switch in PrV, whereas gamma peptides play this role in NomegaV. PrV gamma peptides instead interact with packaged RNA at the particle two-folds by using a repeating sequence pattern found in only four other RNA- or membrane-binding proteins. The disposition of peptide termini in PrV is closely related to those in nodaviruses, suggesting that PrV may be closer to the primordial T = 4 particle than NomegaV. Evolution in action: N and C termini of subunits in related T = 4 viruses exchange roles as molecular switches.,Speir JA, Taylor DJ, Natarajan P, Pringle FM, Ball LA, Johnson JE Structure. 2010 Jun 9;18(6):700-9. PMID:20541507[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|