2gu0
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Crystal Structure of Human Rotavirus NSP2 (Group C / Bristol Strain)
OverviewOverview
Viral inclusion bodies, or viroplasms, that form in rotavirus-infected, cells direct replication and packaging of the segmented double-stranded, RNA (dsRNA) genome. NSP2, one of two rotavirus proteins needed for, viroplasm assembly, possesses NTPase, RNA-binding, and helix-unwinding, activities. NSP2 of the rotavirus group causing endemic infantile diarrhea, (group A) was shown to self-assemble into large doughnut-shaped octamers, with circumferential grooves and deep clefts containing nucleotide-binding, histidine triad (HIT)-like motifs. Here, we demonstrate that NSP2 of group, C rotavirus, a group that fails to reassort with group A viruses, retains, the unique architecture of the group A octamer but differs in surface, charge distribution. By using an NSP2-dependent complementation system, we, show that the HIT-dependent NTPase activity of NSP2 is necessary for dsRNA, synthesis, but not for viroplasm formation. The complementation system, also showed that despite the retention of the octamer structure and the, HIT-like fold, group C NSP2 failed to rescue replication and viroplasm, formation in NSP2-deficient cells infected with group A rotavirus. The, distinct differences in the surface charges on the Bristol and SA11 NSP2, octamers suggest that charge complementarity of the viroplasm-forming, proteins guides the specificity of viroplasm formation and, possibly, reassortment restriction between rotavirus groups.
About this StructureAbout this Structure
2GU0 is a Single protein structure of sequence from Human rotavirus (group c/strain bristol). Full crystallographic information is available from OCA.
ReferenceReference
Structure-function analysis of rotavirus NSP2 octamer by using a novel complementation system., Taraporewala ZF, Jiang X, Vasquez-Del Carpio R, Jayaram H, Prasad BV, Patton JT, J Virol. 2006 Aug;80(16):7984-94. PMID:16873255
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