hydrolase activity, acting on acid anhydrides / Rotavirus non-structural protein 2 / viral genome replication / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / host cell cytoplasm / RNA binding / ATP binding / metal ion binding / Non-structural protein 2
Function and homology information
Biological species
Human rotavirus B strain CAL-1
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å
Journal: J Virol / Year: 2024 Title: Cryo-EM structure of rotavirus B NSP2 reveals its unique tertiary architecture. Authors: Sebastian Chamera / Krzysztof Wycisk / Mariusz Czarnocki-Cieciura / Marcin Nowotny / Abstract: Rotavirus (RV) NSP2 is a multifunctional RNA chaperone that exhibits numerous activities that are essential for replication and viral genome packaging. We performed an analysis that highlighted a ...Rotavirus (RV) NSP2 is a multifunctional RNA chaperone that exhibits numerous activities that are essential for replication and viral genome packaging. We performed an analysis that highlighted a distant relationship of NSP2 from rotavirus B (RVB) to proteins from other human RVs. We solved a cryo-electron microscopy structure of RVB NSP2 that shows structural differences with corresponding proteins from other human RVs. Based on the structure, we identified amino acid residues that are involved in RNA interactions. Anisotropy titration experiments showed that these residues are important for nucleic acid binding. We also identified structural motifs that are conserved in all RV species. Collectively, our data complete the structural characterization of rotaviral NSP2 protein and demonstrate its structural diversity among RV species.IMPORTANCERotavirus B (RVB), also known as adult diarrhea rotavirus, has caused epidemics of severe diarrhea in China, India, and Bangladesh. Thousands of people are infected in a single RVB epidemic. However, information on this group of rotaviruses remains limited. As NSP2 is an essential protein in the viral life cycle, including its role in the formation of replication factories, it may be a target for future antiviral strategy against viruses with similar mechanisms.
A: Non-structural protein 2 B: Non-structural protein 2 C: Non-structural protein 2 D: Non-structural protein 2 E: Non-structural protein 2 F: Non-structural protein 2 G: Non-structural protein 2 H: Non-structural protein 2
Mass: 34575.672 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human rotavirus B strain CAL-1 / Gene: NSP2 / Production host: Escherichia coli (E. coli) References: UniProt: Q6XD98, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
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Experimental details
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Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction
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Sample preparation
Component
Name: Homooctamer of NSP2 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weight
Experimental value: NO
Source (natural)
Organism: Rotavirus B / Strain: Mexico
Source (recombinant)
Organism: Escherichia coli (E. coli)
Details of virus
Isolate: OTHER / Type: VIRION
Buffer solution
pH: 7
Specimen
Conc.: 0.36 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
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