1lj2
Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
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| , resolution 2.38Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
About this StructureAbout this Structure
1LJ2 is a Protein complex structure of sequences from Simian rotavirus a/sa11. Full crystallographic information is available from OCA.
ReferenceReference
Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization., Groft CM, Burley SK, Mol Cell. 2002 Jun;9(6):1273-83. PMID:12086624
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