6n9y

<table><tr><td colspan='2'>[[6n9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bluetongue_virus_23 Bluetongue virus 23]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N9Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6N9Y FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6n9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n9y OCA], [http://pdbe.org/6n9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n9y RCSB], [http://www.ebi.ac.uk/pdbsum/6n9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n9y ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Bluetongue virus (BTV) non-structural protein 1 (NS1) regulates viral protein synthesis and exists as tubular and non-tubular forms in infected cells, but how tubules assemble and how protein synthesis is regulated are unknown. Here, we report near-atomic resolution structures of two NS1 tubular forms determined by cryo-electron microscopy. The two tubular forms are different helical assemblies of the same NS1 monomer, consisting of an amino-terminal foot, a head and body domains connected to an extended carboxy-terminal arm, which wraps atop the head domain of another NS1 subunit through hydrophobic interactions. Deletion of the C terminus prevents tubule formation but not viral replication, suggesting an active non-tubular form. Two zinc-finger-like motifs are present in each NS1 monomer, and tubules are disrupted by divalent cation chelation and restored by cation addition, including Zn(2+), suggesting a regulatory role of divalent cations in tubule formation. In vitro luciferase assays show that the NS1 non-tubular form upregulates BTV mRNA translation, whereas zinc-finger disruption decreases viral mRNA translation, tubule formation and virus replication, confirming a functional role for the zinc-fingers. Thus, the non-tubular form of NS1 is sufficient for viral protein synthesis and infectious virus replication, and the regulatory mechanism involved operates through divalent cation-dependent conversion between the non-tubular and tubular forms.

 

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== References ==

[[Category: Boyce, M]]

[[Category: Ge, P]]

[[Category: Jih, J]]

[[Category: Kerviel, A]]

[[Category: Lai, M]]

[[Category: Roy, P]]

[[Category: Zhang, X]]

[[Category: Zhou, Z H]]

[[Category: Viral protein]]