Molecular features of the sortase enzyme family

Bacteria possess complex and varying cell walls with many surface exposed proteins. Sortases are responsible for the covalent attachment of specific proteins to the peptidoglycan of the cell wall of Gram-positive bacteria. Sortase A of Staphylococcus aureus, which is seen as the archetypal sortase, has been shown to be essential for pathogenesis and has therefore received much attention as a potential target for novel therapeutics. Being widely present in Gram-positive bacteria, it is likely that other Gram-positive pathogens also require sortases for their pathogenesis. Sortases have also been shown to be of significant use in a range of industrial applications. We review current knowledge of the sortase family in terms of their structures, functions and mechanisms and summarize work towards their use as antibacterial targets and microbiological tools. Sortases are responsible for the covalent attachment of proteins to the gram-positive cell wall. Staphylococcus aureus Sortase A has been shown to be required for pathogenesis and has therefore garnered considerable attention as a potential drug target. Here we review current structural, functional and mechanistic knowledge of sortases and efforts to target them therapeutically and exploit them industrially. This article is accompanied by a podcast, listen now. Or listen in iTunes.