<p>The bacterial ribosomal protein L25 is bound to 5S rRNA along with L5 and L18, forming a separate domain of the ribosome [<cite idref="PUB00014122"/>]. 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 <taxon tax_id="274">Thermus thermophilus</taxon> ribosomal protein TL5, to the general stress protein CTC, and to the C-terminal anticodon-binding domain of <taxon tax_id="562">Escherichia coli</taxon> glutaminyl-tRNA synthetase (GlnRS) [<cite idref="PUB00014120"/>, <cite idref="PUB00014121"/>]. GlnRS contains a duplication consisting of two L25-like beta-barrels domains with the swapping of N-terminal strands.</p><p>This entry represents a domain with a mainly beta-strand structure found in ribosomal L25-like proteins.</p>