Journal
PROTEIN SCIENCE
Volume 14, Issue 5, Pages 1350-1356Publisher
WILEY
DOI: 10.1110/ps.051415905
Keywords
esterase; lipase; Yhr049w/FSH1; serine hydrolase; OVCA2; Ymr222c/FSH2; Yor280c/FSH3
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Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine-type hydrolase belonging to the broad functional alpha beta-hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal alpha beta-hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.
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