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- W2024684906 abstract "X-ray structures of the universal translation initiation factor IF2/eIF5B have been determined in three states: free enzyme, inactive IF2/eIF5B·GDP, and active IF2/eIF5B·GTP. The “chalice-shaped” enzyme is a GTPase that facilitates ribosomal subunit joining and Met-tRNAi binding to ribosomes in all three kingdoms of life. The conserved core of IF2/eIF5B consists of an N-terminal G domain (I) plus an EF-Tu-type β barrel (II), followed by a novel α/β/α-sandwich (III) connected via an α helix to a second EF-Tu-type β barrel (IV). Structural comparisons reveal a molecular lever, which amplifies a modest conformational change in the Switch 2 region of the G domain induced by Mg2+/GTP binding over a distance of 90 Å from the G domain active center to domain IV. Mechanisms of GTPase function and ribosome binding are discussed." @default.
- W2024684906 created "2016-06-24" @default.
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- W2024684906 date "2000-11-01" @default.
- W2024684906 modified "2023-10-17" @default.
- W2024684906 title "X-Ray Structures of the Universal Translation Initiation Factor IF2/eIF5B" @default.
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- W2024684906 doi "https://doi.org/10.1016/s0092-8674(00)00181-1" @default.
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