View source for 4rft


==T=1 subviral particle of Grouper nervous necrosis virus capsid protein deletion mutant (delta 1-34 & 218-338)==
<StructureSection load='4rft' size='340' side='right'caption='[[4rft]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rft]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Epinephelus_coioides_nervous_necrosis_virus Epinephelus coioides nervous necrosis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RFT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=4rft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rft OCA], [https://pdbe.org/4rft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rft RCSB], [https://www.ebi.ac.uk/pdbsum/4rft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rft ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8JNX5_9VIRU Q8JNX5_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Betanodaviruses cause massive mortality in marine fish species with viral nervous necrosis. The structure of a T = 3 Grouper nervous necrosis virus-like particle (GNNV-LP) is determined by the ab initio method with non-crystallographic symmetry averaging at 3.6 A resolution. Each capsid protein (CP) shows three major domains: (i) the N-terminal arm, an inter-subunit extension at the inner surface; (ii) the shell domain (S-domain), a jelly-roll structure; and (iii) the protrusion domain (P-domain) formed by three-fold trimeric protrusions. In addition, we have determined structures of the T = 1 subviral particles (SVPs) of (i) the delta-P-domain mutant (residues 35-217) at 3.1 A resolution; and (ii) the N-ARM deletion mutant (residues 35-338) at 7 A resolution; and (iii) the structure of the individual P-domain (residues 214-338) at 1.2 A resolution. The P-domain reveals a novel DxD motif asymmetrically coordinating two Ca2+ ions, and seems to play a prominent role in the calcium-mediated trimerization of the GNNV CPs during the initial capsid assembly process. The flexible N-ARM (N-terminal arginine-rich motif) appears to serve as a molecular switch for T = 1 or T = 3 assembly. Finally, we find that polyethylene glycol, which is incorporated into the P-domain during the crystallization process, enhances GNNV infection. The present structural studies together with the biological assays enhance our understanding of the role of the P-domain of GNNV in the capsid assembly and viral infection by this betanodavirus.

Crystal Structures of a Piscine Betanodavirus: Mechanisms of Capsid Assembly and Viral Infection.,Chen NC, Yoshimura M, Guan HH, Wang TY, Misumi Y, Lin CC, Chuankhayan P, Nakagawa A, Chan SI, Tsukihara T, Chen TY, Chen CJ PLoS Pathog. 2015 Oct 22;11(10):e1005203. doi: 10.1371/journal.ppat.1005203., eCollection 2015 Oct. PMID:26491970<ref>PMID:26491970</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rft" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Epinephelus coioides nervous necrosis virus]]
[[Category: Large Structures]]
[[Category: Chen CJ]]
[[Category: Chen NC]]
[[Category: Chen TY]]
[[Category: Guan HH]]
[[Category: Yoshimura M]]