title: Data on structural transitions in domains of hordeivirus TGB1 protein forming ribonucleoprotein complex.
abstract: This data article is related to the research article entitled "in vitro properties of hordeivirus TGB1 protein forming ribonucleoprotein complexes" (Makarov et al., 2015 [1]), demonstrating that upon incubation with viral RNA the poa semilatent hordeivirus (PSLV) TGB1 protein (the movement 63 K protein encoded by the first gene of the triple gene block) in vitro forms RNP structures resembling filamentous virus-like particles and its internal domain (ID) performs a major structural role in this process. This article reports the additional results on the structural lability of ID and the structural transitions in the C-terminal NTPase/helicase domain (HELD) induced by interaction with tRNA and phosphorylation.
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninsky Gory, Moscow 119992, Russia.
authors.forename: Valentin V
authors.initials: VV
authors.lastname: Makarov
authors.affiliation: Department of Virology, Lomonosov Moscow State University, Leninsky Gory, Moscow 119992, Russia.
authors.forename: Svetlana S
authors.initials: SS
authors.lastname: Makarova
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninsky Gory, Moscow 119992, Russia.
authors.forename: Natalia O
authors.initials: NO
authors.lastname: Kalinina
keywords: Hordeivirus; Plant virus transport; RNP-complexes