The third structural switch in the archaeal translation initiation factor 2 (aif2) molecule and its possible role in the initiation of gtp hydrolysis and the removal of aif2 from the ribosomeстатьяИсследовательская статья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 24 июля 2019 г.
Аннотация:The structure of the gamma subunit of the archaeal translation initiation factor 2 from Sulfolobus solfataricus (SsoIF2gamma) in complex with GDPCP (GTP analog) was determined. Crystals were obtained in the absence of magnesium ions in the crystallization solution. They belong to space group P1. In the unit cell there are five molecules, four of which are related in pairs by a common non-crystallographic 2-fold symmetry axis, and the fifth has no symmetric equivalent. Analysis of the structure and its comparison with other known aIF2gamma structures in GTP-bound state show that 1) the magnesium ion is necessary for the formation and maintenance of the active form of SsoIF2gamma; 2) besides the two previously known structural switches 1 and 2, the e/aIF2 molecules have one more flexible region (switch 3), which function may consist in initiation of hydrolysis of GTP and removal of aIF2 from the ribosome after codon-anticodon recognition.