ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis
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 |