2qqp
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qqp]] is a 9 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2QQP FirstGlance]. <br> | <table><tr><td colspan='2'>[[2qqp]] is a 9 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2QQP FirstGlance]. <br> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</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=2qqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqp OCA], [https://pdbe.org/2qqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qqp RCSB], [https://www.ebi.ac.uk/pdbsum/2qqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqp ProSAT]</span></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=2qqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqp OCA], [https://pdbe.org/2qqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qqp RCSB], [https://www.ebi.ac.uk/pdbsum/2qqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q80IX5_PRVFL Q80IX5_PRVFL] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The 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. | ||
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| - | 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<ref>PMID:20541507</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2qqp" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Providence virus]] | [[Category: Providence virus]] | ||
| - | [[Category: Johnson | + | [[Category: Johnson JE]] |
| - | [[Category: Speir | + | [[Category: Speir JA]] |
| - | [[Category: Taylor | + | [[Category: Taylor DJ]] |
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Current revision
Crystal Structure of Authentic Providence Virus
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