Aspergillus niger protein estA defines a new class of fungal esterases within the alfa/beta hydrolase fold superfamily of proteins

Y. Bourne, A.A. Hasper, H. Chahinian, M. Juin, L.H. de Graaff

Research output: Contribution to journalArticleAcademicpeer-review

20 Citations (Scopus)

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 lipaseacetylcholinesterase 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.
Original languageEnglish
Pages (from-to)677-687
JournalStructure
Volume12
Issue number8
DOIs
Publication statusPublished - 2004

Keywords

  • transcriptional activator xlnr
  • 3-dimensional structure
  • acetylxylan esterase
  • antifungal agents
  • gene-expression
  • vinyl esters
  • sequence
  • acetylcholinesterase
  • lipases
  • refinement

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