Fig. 6: Potential RNA binding surface of the G5C decamer.
From: Structural basis for Gemin5 decamer-mediated mRNA binding
a In the structure of the G5C decamer, B–B’ and C–C’ are two spatially adjacent dimers, with B, B’, C, and C’ colored cyan, green, pink, and yellow, respectively. b Electrostatic surface of the two adjacent dimers, B–B’ and C–C’. c Close-up view of a large positively charged concave surface as the potential RNA binding site formed by the TPR domain of molecule B (TPRB) and the RBS1 region of molecule C (RBS1C). The four basic TPR residues within α13–α17, including R1035, K1061, K1062, and R1090, are shown in sticks. TPRB and RBS1C are indicated. Two invisible loops in molecule C are indicated by dashes. d SEC and e EMSA for the G5C mutant R1035A/K1061A/K1062A/R1090A. f SEC assay for G5C A951E. For Fig. 6d–f, each experiment was repeated independently twice with similar results. g FP assay for WT G5C, A951E, and M4 binding to SL1 RNA with the indicated KD values. Data represented as mean ± SD (n = 2 per concentration and two individual experiments).
