Structure of a feruloyl esterase from Aspergillus niger

Authors: McAuley, Katherine E.; Svendsen, Allan; Patkar, Shamkant A.; Wilson, Keith S.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 878-887(10)

Publisher: Blackwell Publishing

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 Å by molecular replacement. The protein has an α/β-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 Å and reveals dual conformations for the serine and histidine residues at the active site.

Keywords: feruloyl esterase; ferulic acid esterase; ACORN; molecular replacement

Document Type: Research article

DOI: 10.1107/S0907444904004937

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.16 plus tax Refund Policy