5nd1: Difference between revisions

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'''Unreleased structure'''


The entry 5nd1 is ON HOLD
==Viral evolution results in multiple, surface-allocated enzymatic activities in a fungal double-stranded RNA virus==
<SX load='5nd1' size='340' side='right' viewer='molstar' caption='[[5nd1]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nd1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rosellinia_necatrix_quadrivirus_1 Rosellinia necatrix quadrivirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ND1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ND1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</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=5nd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nd1 OCA], [https://pdbe.org/5nd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nd1 RCSB], [https://www.ebi.ac.uk/pdbsum/5nd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nd1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M1VMJ0_RNQV1 M1VMJ0_RNQV1]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 A resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-A-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar alpha-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.


Authors:  
Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.,Mata CP, Luque D, Gomez-Blanco J, Rodriguez JM, Gonzalez JM, Suzuki N, Ghabrial SA, Carrascosa JL, Trus BL, Caston JR PLoS Pathog. 2017 Dec 8;13(12):e1006755. doi: 10.1371/journal.ppat.1006755., eCollection 2017 Dec. PMID:29220409<ref>PMID:29220409</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5nd1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Rosellinia necatrix quadrivirus 1]]
[[Category: Carrascosa JL]]
[[Category: Caston JR]]
[[Category: Ghabrial SA]]
[[Category: Gomez Blanco J]]
[[Category: Luque D]]
[[Category: Mata CP]]
[[Category: Rodriguez JM]]
[[Category: Suzuki N]]
[[Category: Trus BL]]

Latest revision as of 12:48, 15 November 2023

Viral evolution results in multiple, surface-allocated enzymatic activities in a fungal double-stranded RNA virus

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