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The structural features of an ancient ribonuclease from Salmo salar reveal an intriguing case of auto-inhibition

Int J Biol Macromol. 2021-04; 
Filomena Sica, Irene Russo Krauss, Romualdo Troisi, Andrea Bosso, Rosanna Culurciello, Carla Carluccio, Mariateresa Trapani, Antonello Merlino, Lelio Mazzarella, Elio Pizzo
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摘要

The superfamily of vertebrate ribonucleases, a large group of evolutionarily related proteins, continues to provide interesting structural and functional information. In particular, the crystal structure of SS-RNase-2 from Salmo salar (SS2), here presented, has revealed a novel auto-inhibition mechanism that enriches the number of inhibition strategies observed in some members of the family. Within an essentially unmodified RNase folding, the SS2 active site cleft is in part obstructed by the collapse of an extra pentapeptide inserted in the C-terminal region. This unexpected intrusion alters the organization of the catalytic triad by pushing one catalytic histidine off the pocket. Possible mechanisms to remove... More

关键词

Auto-inhibition, Crystal structure, Evolution, Ribonucleases