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

Chilton, Annemarie S.
Ellis, Ashley L.
Lamb, Audrey L.
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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.
Description
This is the published version.
Date
2014-10-08
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Publisher
International Union of Crystallography
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Keywords
Ergot alkaloid, Old yellow enzyme, EasA, FgaOx3, Aspergillus fumigatus
Citation
Chilton, Annemarie S., Ashley L. Ellis, and Audrey L. Lamb. "Structure of an Aspergillus Fumigatus Old Yellow Enzyme (EasA) Involved in Ergot Alkaloid Biosynthesis." Acta Cryst Sect F Acta Cryst Sect F Struct Biol Commun Acta Crystallogr F Struct Biol Cryst Commun Acta Crystallogr Sect F Struct Biol Commun Acta Crystallogr F Struct Biol Commun Acta Cryst F Struct Biol Commun Acta Cryst F Acta Crystallogr F Acta Crystallographica Section F Structural Biology Communications Acta Crystallogr Sect F Acta Crystallogr Sect F Struct Biol Cryst Commun 70.10 (2014): 1328-332. http://dx.doi.org/10.1107/S2053230X14018962
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