Conserved residues are critical for Haloferax volcanii archaeosortase catalytic activity: implications for convergent evolution of the catalytic mechanisms of non ‐homologous sortases from archaea and bacteria

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Although evolutionarily unrelated, bacterial sortases and archaeal archaeosortases both recognize and process the C‐termini of substrates having similar tripartite structures, followed by covalent attachment to the cell surface via the newly generated C‐termini. Here, we show that, similar to the sortase, the archaeosortase active site contains a catalytic triad of amino acids that processes the substrates. However, in archaeosortases, but not sortases, these residues appear to be located within three conserved transmembrane segments.

Source: Molecular Microbiology - February 21, 2018 Category: Microbiology Authors: Mohd Farid Abdul Halim, Ronald Rodriguez, Jonathan D. Stoltzfus, Iain G. Duggin, Mechthild Pohlschroder Tags: Research Article Source Type: research