2qqp: Difference between revisions

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<SX load='2qqp' size='340' side='right' viewer='molstar' caption='[[2qqp]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<SX load='2qqp' size='340' side='right' viewer='molstar' caption='[[2qqp]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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 [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"><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]] 3.8&#8491;</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>
<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>
</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.
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>
From MEDLINE&reg;/PubMed&reg;, 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 protein|Virus coat protein]]
*[[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, J E]]
[[Category: Johnson JE]]
[[Category: Speir, J A]]
[[Category: Speir JA]]
[[Category: Taylor, D J]]
[[Category: Taylor DJ]]
[[Category: Auto proteolysis]]
[[Category: Auto-catalytic cleavage]]
[[Category: Beta barrel]]
[[Category: Capsid]]
[[Category: Coat protein]]
[[Category: Icosahedral virus]]
[[Category: Ig-like domain]]
[[Category: Protein-rna complex]]
[[Category: Quasiequivalence]]
[[Category: Tetraviridae]]
[[Category: Tetravirus]]
[[Category: Virus]]

Latest revision as of 12:17, 21 February 2024

Crystal Structure of Authentic Providence VirusCrystal Structure of Authentic Providence Virus

2qqp, resolution 3.80Å

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