InterPro domain: IPR020056

The bacterial ribosomal protein L25 is bound to 5S rRNA along with L5 and L18, forming a separate domain of the ribosome [ 1 ]. The solution structure of protein L25 uncomplexed with RNA shows two significantly disordered loops and a closed beta-barrel domain with a complex topology that has significant structural similarities to the N-terminal domain of the Thermus thermophilus ribosomal protein TL5, to the general stress protein CTC, and to the C-terminal anticodon-binding domain of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) [ 2 , 3 ]. GlnRS contains a duplication consisting of two L25-like beta-barrels domains with the swapping of N-terminal strands.

This superfamily represents the N-terminal domain, which has a beta-barrel structure.

1. Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution. Proc. Natl. Acad. Sci. U.S.A. 97, 2023-8
2. Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins. Acta Crystallogr. D Biol. Crystallogr. 57, 968-76
3. tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase. Structure 11, 591-603