1YCD

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

1YCD の概要

• エントリーDOI: 10.2210/pdb1ycd/pdb
• 分子名称: Hypothetical 27.3 kDa protein in AAP1-SMF2 intergenic region, 2-HYDROXY-4,5-DIOXOHEPTYL HYDROGEN PHOSPHONATE (3 entities in total)
• 機能のキーワード: esterase, lipase, serine hydrolase, s. cerevisiae, structural genomics, paris-sud yeast structural genomics, ysg, unknown function
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm : P38777
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55132.70

構造登録者

Leulliot, N.,Graille, M.,Coste, F.,Quevillon-Cheruel, S.,Janin, J.,van Tilbeurgh, H.,Paris-Sud Yeast Structural Genomics (YSG) (登録日: 2004-12-22, 公開日: 2005-05-10, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)