dc.contributor.author | Chilton, Annemarie S. | |
dc.contributor.author | Ellis, Ashley L. | |
dc.contributor.author | Lamb, Audrey L. | |
dc.date.accessioned | 2015-12-29T16:50:39Z | |
dc.date.available | 2015-12-29T16:50:39Z | |
dc.date.issued | 2014-10-08 | |
dc.identifier.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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/19334 | |
dc.description | This is the published version. | en_US |
dc.description.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. | en_US |
dc.publisher | International Union of Crystallography | en_US |
dc.subject | Ergot alkaloid | en_US |
dc.subject | Old yellow enzyme | en_US |
dc.subject | EasA | en_US |
dc.subject | FgaOx3 | en_US |
dc.subject | Aspergillus fumigatus | en_US |
dc.title | Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis | en_US |
dc.type | Article | |
kusw.kuauthor | Lamb, Audrey Lee | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1107/S2053230X14018962 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess | |