Structure of archaeal translational initiation factor 2 beta{gamma}-GDP reveals significant conformational change of the beta-subunit and switch 1 region -- Sokabe et al. 103 (35): 13016 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Sokabe et al. 10.1073/pnas.0604165103.

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Fig. 5. Met-tRNA_i affinity assay. (A-H) Saturation curves against Met-tRNA_i of wild-type (A), gT34V (T36) (B), g39-43A (41-45) (C), gE39A (E41) (D), gE40A (E42) (E), gL41A (L43) (F), gK42A (R44) (G), and gR43A (R45) (H) mutants of SsIF2 heterotrimer in the presence of 1 mM GTP at 62°C. g39-43A and gE40A mutations severely impair Met-tRNA_i binding, and gT34V impairs it slightly; the others had little effect in the presence of GTP. (I-K) Saturation curves against Met-tRNA_i of wild-type abg (I), bR86M (R87) mutant of abg (J), and wild-type ag dimer (K) in the presence of 1 mM GDP at 62°C (the residues in parentheses indicate the corresponding residue in PfIF2). bR86M mutation or the absence of the b-subunit had little effect in the presence of GDP. Each point represents the mean of three independent experiments, except for C, which shows the plot of a single experiment. Error bars indicate SD.