Structure of the SAM-II riboswitch bound to S-adenosylmethionine

More documents

Recommendations

Info

Supplementary Figure 4 Superposition of the three protomers in the asymmetric unit that were built and refined individually. The standard pairwise r.m.s.d. for all atoms in the RNA and SAM is 1.26 Å and the maximum likelihood r.m.s.d. for all atoms is 0.19 Å, as calculated using the program THESEUS 20 . The two perspectives correspond to (a) Figure 1b and (b) Figure 1c (Figure 1b, c shows protomer A). Colors correspond to: red, molecule A; blue, molecule B; green, molecule C, as defined in the PDB coordinate file.
Supplementary Figure 5 Comparison of A-minor twist motifs in SAM-II riboswitch (left) and glmS ribozymes (right) 18,19 . Watson-Crick paired helical regions are colored in blue. A-minor twist interaction is colored in magenta. The glmS model and numbering shown was created from the Glc6P-bound 2’-deoxy precleavage structure of the glmS ribozyme from T. tencongensis (PDB ID 2h0z) 19 .
Page 1 and 2: Structure of the SAM-II riboswitch
Page 3 and 4: Supplementary Figure 2 SAM binding
Page 8 and 9: Supplementary Figure 6 Raw data obt
Page 10 and 11: Supplementary Table 1: Sequence ali
Page 12 and 13: formamide, xylene cyanol, and bromo
Page 14 and 15: of merit improved to 0.35. An exper
Page 16 and 17: negative control. Reactions were al
Page 18 and 19: per lane 12 . Normalizing to differ
Page 20 and 21: References. 1. Corbino, K.A. et al.

Structure of the SAM-II riboswitch bound to S-adenosylmethionine

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?