The NMR structure of the 5S rRNA E-domain–protein L25 complex shows preformed and induced recognition

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Abstract
The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E‐loop and helix IV regions of the E‐domain of Escherichia coli 5S rRNA, has been determined to an overall r.m.s. displacement of 1.08 Å (backbone heavy atoms) by heteronuclear NMR spectroscopy (Protein Databank code 1d6k). The interacting molecular surfaces are bipartite for both the RNA and the protein. One side of the six‐stranded β‐barrel of L25 recognizes the minor groove of the E‐loop with very little change in the conformations of either the protein or the RNA and with the RNA–protein interactions occurring mainly along one strand of the E‐loop duplex. This minor groove recognition module includes two parallel β‐strands of L25, a hitherto unknown RNA binding topology. Binding of the RNA also induces conversion of a flexible loop to an α‐helix in L25, the N‐terminal tip of which interacts with the widened major groove at the E‐loop/helix IV junction of the RNA. The structure of the complex reveals that the E‐domain RNA serves as a preformed docking partner, while the L25 protein has one preformed and one induced recognition module.