|Entry||Database: EMDB / ID: EMD-0383|
|Title||Atomic structure of Non-Structural protein 1 of bluetongue virus|
|Sample||Non-structural protein 1 (tubule):|
Non-structural protein 1
|Function / homology||Orbivirus non-structural protein NS1/hydrophobic tubular protein / NS1|
Function and homology information
|Biological species||Bluetongue virus (serotype 1 / isolate South Africa) / Bluetongue virus 23|
|Method||helical reconstruction / cryo EM / Resolution: 4 Å|
|Authors||Kerviel A / Ge P / Lai M / Jih J / Boyce M / Zhang X / Zhou ZH / Roy P|
|Funding support|| United States, United Kingdom, 3 items |
|Citation||Journal: Nat Microbiol / Year: 2019|
Title: Atomic structure of the translation regulatory protein NS1 of bluetongue virus.
Authors: Adeline Kerviel / Peng Ge / Mason Lai / Jonathan Jih / Mark Boyce / Xing Zhang / Z Hong Zhou / Polly Roy /
Abstract: 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 ...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, 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.
|Validation Report||PDB-ID: 6n9y|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0383.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.07 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Non-structural protein 1 (tubule)
|Entire||Name: Non-structural protein 1 (tubule) / Number of components: 2|
-Component #1: protein, Non-structural protein 1 (tubule)
|Protein||Name: Non-structural protein 1 (tubule) / Recombinant expression: No|
|Source||Species: Bluetongue virus (serotype 1 / isolate South Africa)|
-Component #2: protein, Non-structural protein 1
|Protein||Name: Non-structural protein 1 / Number of Copies: 1 / Recombinant expression: No|
|Mass||Theoretical: 64.554984 kDa|
|Source||Species: Bluetongue virus 23|
|Specimen||Specimen state: helical array / Method: cryo EM|
|Helical parameters||Axial symmetry: D2 (2x2 fold dihedral) / Delta z: 8.83 Å / Delta phi: -17.5 %deg;|
|Sample solution||pH: 7.5|
|Vitrification||Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 60 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Energy filter: GIF Quantum LS|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 QUANTUM (4k x 4k)|
|Image acquisition||Number of digital images: 5006|
|Processing||Method: helical reconstruction|
|3D reconstruction||Algorithm: BACK PROJECTION / Software: RELION / Resolution: 4 Å / Resolution method: OTHER|
-Atomic model buiding
|Modeling #1||Refinement space: REAL|
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