1ycd
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Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family
OverviewOverview
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, alphabeta-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.
About this StructureAbout this Structure
1YCD is a Single protein structure of sequence from Saccharomyces cerevisiae with LI5 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family., Quevillon-Cheruel S, Leulliot N, Graille M, Hervouet N, Coste F, Benedetti H, Zelwer C, Janin J, Van Tilbeurgh H, Protein Sci. 2005 May;14(5):1350-6. Epub 2005 Mar 31. PMID:15802654
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