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Aspergillus niger Protein EstA Defines a New Class of Fungal Esterases within the α/β Hydrolase Fold Superfamily of Proteins

Abstract : From the fungus Aspergillus niger, we identified a new gene encoding protein EstA, a member of the alpha/beta-hydrolase fold superfamily but of unknown substrate specificity. EstA was overexpressed and its crystal structure was solved by molecular replacement using a lipase-acetylcholinesterase chimera template. The 2.1 A resolution structure of EstA reveals a canonical Ser/Glu/His catalytic triad located in a small pocket at the bottom of a large solvent-accessible, bowl-shaped cavity. Potential substrates selected by manual docking procedures were assayed for EstA activity. Consistent with the pocket geometry, preference for hydrolysis of short acyl/propyl chain substrates was found. Identification of close homologs from the genome of other fungi, of which some are broad host-range pathogens, defines EstA as the first member of a novel class of fungal esterases within the superfamily. Hence the structure of EstA constitutes a lead template in the design of new antifungal agents directed toward its pathogenic homologs.
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https://hal-amu.archives-ouvertes.fr/hal-03263177
Contributor : Julien Caugant <>
Submitted on : Thursday, June 17, 2021 - 9:18:13 AM
Last modification on : Friday, July 2, 2021 - 8:44:01 AM

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Yves Bourne, Alinda Hasper, Henri Chahinian, Marianick Juin, Leo de Graaff, et al.. Aspergillus niger Protein EstA Defines a New Class of Fungal Esterases within the α/β Hydrolase Fold Superfamily of Proteins. Structure, Elsevier (Cell Press), 2004, 12, pp.677 - 687. ⟨10.1016/j.str.2004.03.005⟩. ⟨hal-03263177⟩

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