4qnw | pdb_00004qnw
From Proteopedia
Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus
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Structural highlights
Publication Abstract from PubMedThe 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 A resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the alpha/beta-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. Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis.,Chilton AS, Ellis AL, Lamb AL Acta Crystallogr F Struct Biol Commun. 2014 Oct 1;70(Pt 10):1328-32. doi:, 10.1107/S2053230X14018962. Epub 2014 Sep 25. PMID:25286934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 16:29, 11 August 2016.