Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activities.

ABSTRACT: Rotavirus NSP2 is an abundant non-structural RNA-binding protein essential for forming the viral factories that support replication of the double-stranded RNA genome. NSP2 exists as stable doughnut-shaped octamers within the infected cell, representing the tail-to-tail interaction of two tetramers. Extending diagonally across the surface of each octamer are four highly basic grooves that function as binding sites for single-stranded RNA. Between the N and C-terminal domains of each monomer is a deep electropositive cleft containing a catalytic site that hydrolyzes the gamma-beta phosphoanhydride bond of any NTP. The catalytic site has similarity to those of the histidine triad (HIT) family of nucleotide-binding proteins. Due to the close proximity of the grooves and clefts, we investigated

SUBMITTER: Vasquez-Del Carpio R 

PROVIDER: S-EPMC1924841 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature