|Entry||Database: EMDB / ID: EMD-21531|
|Title||Head masked 3D refined density of the Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit used to build the 5-UTR IRES model|
|Sample||Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit from a head masked 3D refinement|
|Biological species||Oryctolagus cuniculus (rabbit)|
|Method||single particle reconstruction / cryo EM / Resolution: 2.79 Å|
|Authors||Neupane R / Pisareva V / Rodriguez CF / Pisarev A / Fernandez IS|
|Funding support|| United States, 1 items |
|Citation||Journal: Elife / Year: 2020|
Title: A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S complex via an uAUG intermediate.
Authors: Ritam Neupane / Vera P Pisareva / Carlos F Rodriguez / Andrey V Pisarev / Israel S Fernández /
Abstract: Taking control of the cellular apparatus for protein production is a requirement for virus progression. To ensure this control, diverse strategies of cellular mimicry and/or ribosome hijacking have ...Taking control of the cellular apparatus for protein production is a requirement for virus progression. To ensure this control, diverse strategies of cellular mimicry and/or ribosome hijacking have evolved. The initiation stage of translation is especially targeted as it involves multiple steps and the engagement of numerous initiation factors. The use of structured RNA sequences, called nternal ibosomal ntry ites (IRES), in viral RNAs is a widespread strategy for the exploitation of eukaryotic initiation. Using a combination of electron cryo-microscopy (cryo-EM) and reconstituted translation initiation assays with native components, we characterized how a novel IRES at the 5'-UTR of a viral RNA assembles a functional initiation complex via an uAUG intermediate. The IRES features a novel extended, multi-domain architecture, that circles the 40S head. The structures and accompanying functional data illustrate the importance of 5'-UTR regions in translation regulation and underline the relevance of the untapped diversity of viral IRESs.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_21531.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.0605 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Projections & Slices|
-Additional map: Unsharpened map before post-processing for head masked
|Annotation||Unsharpened map before post-processing for head masked|
|Projections & Slices|
-Half map: Half map 1 for head masked
|Annotation||Half map 1 for head masked|
|Projections & Slices|
-Half map: Half map 2 for head masked
-Entire Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the...
|Entire||Name: Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit from a head masked 3D refinement|
Number of components: 1
-Component #1: protein, Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bou...
|Protein||Name: Cricket Paralysis Virus 5-UTR IRES (CrPV 5-UTR-IRES) bound to the small ribosomal subunit from a head masked 3D refinement|
Recombinant expression: No
|Source||Species: Oryctolagus cuniculus (rabbit)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277.15 K / Humidity: 100 %|
Details: Grids were blotted for 2.5s and flash cooled in liquid 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: 56.9 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
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