The ribosomal maturation factor P from facilitates the ribosomal biogenesis by binding to the small ribosomal protein S12.

The ribosomal maturation factor P (RimP) is a highly conserved protein in bacteria and has been shown to be important in ribosomal assembly in Because of its central importance in bacterial metabolism, RimP represents a good potential target for drug design to combat human pathogens such as However, to date, the only RimP structure available is the NMR structure of the ortholog in another bacterial pathogen, Here, we report a 2.2 Å resolution crystal structure of MSMEG_2624, the RimP ortholog in the close relative , and using binding assays, we show that MSMEG_2624 interacts with the small ribosomal protein S12, also known as RpsL. Further analyses revealed that the conserved residues in the linker region between the N- and C-terminal domains of MSMEG_2624 are essential for binding to RpsL. However, neither of the two domains alone was sufficient to form strong interactions with RpsL. More importantly, the linker region was essential for ribosomal biogenesis. Our study provides critical mechanistic insights into the role of RimP in ribosome biogenesis. We anticipate that the MSMEG_2624 crystal structure has the potential to be used for drug design to manage infections.