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Conference papers

New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins

Abstract : The structural alpha/beta-hydrolase fold is characterized by a beta-sheet core of five to eight strands connected by alpha-helices to form a alpha/beta/alpha sandwich. The superfamily members, exemplified by the cholinesterases, diverged from a common ancestor into a number of hydrolytic enzymes displaying a wide range of substrate specificities, along with proteins with no recognized hydrolytic activity. In the enzymes, the catalytic triad residues are presented on loops of which one, the nucleophile elbow, is the most conserved feature of the fold. Of the other proteins, which all lack from one to all of the catalytic residues, some may simply be 'inactive' enzymes while others have been shown to be involved in heterologous surface recognition functions. The ESTHER (for esterases, alpha/beta-hydrolase enzymes and relatives) database (http://bioweb.ensam.inra.fr/esther) gathers and annotates all the published pieces of information (gene and protein sequences; biochemical, pharmacological, and structural data) related to the superfamily, and connects them together to provide the bases for studying structure-function relationships within the superfamily. The most recent developments of the database are presented.
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Submitted on : Thursday, June 4, 2020 - 8:03:20 AM
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Ludovic Renault, Vincent Negre, Thierry Hotelier, Xavier Cousin, P. Marchot, et al.. New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins. 8. International Meeting on Cholinesterases, Sep 2004, Perugia, Italy. ⟨10.1016/j.cbi.2005.10.100⟩. ⟨hal-02764503⟩



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