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Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1328-32. doi: 10.1107/S2053230X14018962. Epub 2014 Sep 25.

Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis.

Author information

1
Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.

Abstract

The Aspergillus fumigatus old yellow enzyme (OYE) EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways. The crystal structure of the FMN-loaded EasA was determined to 1.8 Å resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the α/β-unsaturated aldehyde. The C-terminal tail of one monomer packs into the active site of a monomer in the next asymmetric unit, which is most likely to be a crystallization artifact and not a mechanism of self-regulation.

KEYWORDS:

Aspergillus fumigatus; EasA; FgaOx3; ergot alkaloid; old yellow enzyme

PMID:
25286934
PMCID:
PMC4188074
DOI:
10.1107/S2053230X14018962
[Indexed for MEDLINE]
Free PMC Article

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