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- W1966715771 abstract "Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2 of Bacillus stearothermophilus and provide evidence that this isolated domain binds the 50 S ribosomal subunit and hydrolyzes GTP. Differences between the free and GDP-bound structures of IF2-G2 suggest that domain reorganization within the G2-G3-C1 regions underlies the different structural requirements of IF2 during the initiation process. However, these structural signals are unlikely forwarded from IF2-G2 to the C-terminal fMet-tRNA binding domain (IF2-C2) because the connected IF2-C1 and IF2-C2 modules show completely independent mobility, indicating that the bacterial interdomain connector lacks the rigidity that was found in the archaeal IF2 homolog aIF5B." @default.
- W1966715771 created "2016-06-24" @default.
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- W1966715771 date "2012-03-01" @default.
- W1966715771 modified "2023-09-30" @default.
- W1966715771 title "Structural Dynamics of Bacterial Translation Initiation Factor IF2" @default.
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- W1966715771 doi "https://doi.org/10.1074/jbc.m111.333393" @default.
- W1966715771 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3322840" @default.
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