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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.

More information Original publication

DOI

10.1111/febs.13288

Type

Journal article

Publication Date

2015-06-01T00:00:00+00:00

Volume

282

Pages

2097 - 2114

Total pages

17

Keywords

crystal structure, inhibitor design, molecular mechanism, peptide recognition, sortase, Aminoacyltransferases, Animals, Anti-Bacterial Agents, Bacteria, Bacterial Infections, Bacterial Proteins, Cysteine Endopeptidases, Humans, Protein Binding, Protein Conformation, Species Specificity, Substrate Specificity