Fig. 5. Ribbon representations indicating the structural diversity of protein–K-turn complexes found in the structure of the H.marismortui 50S subunit. (A) L24 and L29 interact with opposite sides of KT-7. (B) Helical fragments of L10 bind to the bulged nucleotide in KT-42. (C) L19e and L37Ae make limited interactions with KT-58. (D) The β-extension of L4 interacts through the widened major groove of KT-46’s C-stem, while L32e recognizes its kinked backbone and protruded base. (E) L7Ae and L15e surround KT-15 with the majority of interactions involving hydrophobic packing made possible by the severe bend in the RNA helix.