1YCD

Crystal structure of yeast FSH1/YHR049W, a member of the serine hydrolase family

Summary for 1YCD

• Entry DOI: 10.2210/pdb1ycd/pdb
• Descriptor: Hypothetical 27.3 kDa protein in AAP1-SMF2 intergenic region, 2-HYDROXY-4,5-DIOXOHEPTYL HYDROGEN PHOSPHONATE (3 entities in total)
• Functional Keywords: esterase, lipase, serine hydrolase, s. cerevisiae, structural genomics, paris-sud yeast structural genomics, ysg, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P38777
• Total number of polymer chains: 2
• Total formula weight: 55132.70

Authors

Leulliot, N.,Graille, M.,Coste, F.,Quevillon-Cheruel, S.,Janin, J.,van Tilbeurgh, H.,Paris-Sud Yeast Structural Genomics (YSG) (deposition date: 2004-12-22, release date: 2005-05-10, Last modification date: 2024-10-30)

Primary citation

Quevillon-Cheruel, S.,Leulliot, N.,Graille, M.,Hervouet, N.,Coste, F.,Zelwer, C.,Janin, J.,Van Tilbeurgh, H.
Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family.
Protein Sci., 14:1350-1356, 2005

PubMed Abstract: 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.

PubMed: 15802654
DOI: 10.1110/ps.051415905

Experimental method

X-RAY DIFFRACTION (1.7 Å)