InterPro domain: IPR035911

The MurF protein contains three domains. The N-terminal domain consists of a small alpha/beta fold and contacts the larger central domain across a broad hydrophobic interface. The central domain and the C-terminal domain adopt mononucleotide and dinucleotide (Rossmann) folds, respectively, and are connected by a short linker peptide that is poorly ordered in the crystal [ 1 ].

This superfamily represents the N-terminal domain of the MurE/F proteins. They are ligases involved in the formation of UDP-N-acetylmuramyl-pentapeptide [ 2 ] and have been considered as antibacterial targets [ 2 ].

1. Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure. Protein Sci. 14, 3039-47
2. Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F. Bioorg. Chem. 55, 2-15