| Title : Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha\/beta hydrolase fold superfamily of proteins - Bourne_2004_Structure_12_677 |
| Author(s) : Bourne Y , Hasper AA , Chahinian H , Juin M , De Graaff LH , Marchot P |
| Ref : Structure , 12 :677 , 2004 |
| 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. |
| ESTHER : Bourne_2004_Structure_12_677 |
| PubMedSearch : Bourne_2004_Structure_12_677 |
| PubMedID: 15062090 |
| Gene_locus related to this paper: aspni-EstA |
| Gene_locus related to this paper: aspni-EstA |
Bourne Y, Hasper AA, Chahinian H, Juin M, De Graaff LH, Marchot P (2004)
Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha\/beta hydrolase fold superfamily of proteins
Structure
12 :677
Bourne Y, Hasper AA, Chahinian H, Juin M, De Graaff LH, Marchot P (2004)
Structure
12 :677