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. 2016 Feb 1;27(3):588–598. doi: 10.1091/mbc.E15-09-0621

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© 2016 Whitfield et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 5: — Mil1 has a conserved serine hydrolase catalytic triad. (A) BLAST alignment of the conserved DUF726 domain in Mil1. Intensity of blue-highlighted residues corresponds to percentage identity. Conserved residues corresponding to the predicted Ser-Asp-His catalytic triad are highlighted in red. (B) Structural model showing the catalytic triad of the well-characterized lipase B from C. antarctica (left; Protein Data Bank ID: 1TCA) and the Phyre2 homology model showing the predicted catalytic triad of Mil1 (right). (C) Sertraline sensitivity was assessed by plating strains in a 10× dilution series on YPD containing 22.5 μM sertraline or DMSO as a control.